Method of Detecting an Endotoxin Using Limulus Amebocyte Lysate Substantially Free of Coagulogen

The present invention is related to a method of detecting an endotoxin in a sample using a chromogenic assay, the method comprising: (a) contacting the sample with a reagent comprising amebocyte lysate (LAL) and a chromogenic substrate; and (b) measuring a chromogenic effect resulting from a change in the chromogenic substrate in the presence of endotoxin in the sample; wherein the LAL is substantially free of coagulogen. The method also relates to compositions and kits comprising LAL substantially free of coagulogen, and methods of making such. 1. A method of detecting an endotoxin in a sample using a chromogenic assay , the method comprising:{'i': 'limulus', 'a. contacting the sample with a reagent comprising amebocyte lysate (LAL) and a chromogenic substrate;'}b. measuring a chromogenic effect resulting from a change in the chromogenic substrate in the presence of endotoxin in the sample;wherein the LAL is substantially free of coagulogen.2. (canceled)3. The method of claim 1 , wherein the chromogenic substrate is Ac-Ile-Glu-Ala-Arg-pNA.4. The method of claim 1 , wherein the change in the chromogenic substrate occurs due to an enzymatic reaction.5. The method of claim 1 , wherein the enzymatic reaction is cleavage of a chromophore from a polypeptide.6. (canceled)7. (canceled)8. (canceled)9. The method of claim 1 , wherein the reagent is an aqueous liquid.10. (canceled)11. The method of claim 1 , wherein the LAL is lyophilized claim 1 , and then reconstituted prior to contacting with the sample.12. The method of claim 1 , wherein the chromogenic substrate is lyophilized claim 1 , and then reconstituted prior to contacting with the sample.13. (canceled)14. The method of claim 1 , wherein the sample is selected from the group consisting of a parenteral dosage form claim 1 , vaccine claim 1 , antibiotic claim 1 , therapeutic protein claim 1 , therapeutic nucleic acid claim 1 , therapeutic antibody claim 1 , and biological product.15. The method of claim 1 , wherein ...

METHOD OF DETECTING AN ENDOTOXIN USING LIMULUS AMEBOCYTE LYSATE SUBSTANTIALLY FREE OF COAGULOGEN

The present invention is related to a method of detecting an endotoxin in a sample using a chromogenic assay, the method comprising: (a) contacting the sample with a reagent comprising limulus amebocyte lysate (LAL) and a chromogenic substrate; and (b) measuring a chromogenic effect resulting from a change in the chromogenic substrate in the presence of endotoxin in the sample; wherein the LAL is substantially free of coagulogen. The method also relates to compositions and kits comprising LAL substantially free of coagulogen, and methods of making such. 1. A method of making limulus amebocyte lysate (LAL) substantially free of coagulogen , comprising:subjecting a composition comprising LAL, wherein the LAL comprises coagulogen, to tangential flow filtration (TFF) using a 20 kDa to 50 kDa TFF filter, wherein the TFF produces a retentate and a filtrate; andcollecting the retentate, thereby obtaining the LAL substantially free of coagulogen.2. The method of claim 1 , wherein the TFF is performed at a flow rate of 300 ml/min to 600 ml/min.3. The method of claim 2 , wherein the TFF is performed at a flow rate of 350 ml/min to 500 ml/min.4. The method of claim 1 , wherein the composition comprising LAL is in a buffer.5. The method of claim 4 , wherein the buffer is a Tris buffer or IVIES buffer.6. The method of claim 4 , wherein the buffer has a pH of about 6.0 to about 9.0.7. The method of claim 6 , wherein the buffer has a pH of about 7.0 to about 8.0.8. The method of claim 1 , wherein the TFF filter comprises a membrane selected from modified polyethersulfone (mPES) claim 1 , polysulfone (PS) and polyethersulphone (PES).9. The method of claim 8 , wherein the TFF filter comprises a mPES membrane filter.10. The method of claim 1 , wherein the LAL substantially free of coagulogen comprises less than 5% (wt/wt) of coagulogen relative to total protein in the LAL as measured by SDS-PAGE with protein stain.11. The method of claim 10 , wherein the LAL substantially free of ...

UNBIASED DNA METHYLATION MARKERS DEFINE AN EXTENSIVE FIELD DEFECT IN HISTOLOGICALLY NORMAL PROSTATE TISSUES ASSOCIATED WITH PROSTATE CANCER: NEW BIOMARKERS FOR MEN WITH PROSTATE CANCER

A method of detecting the presence of a prostate cancer field defect in a human subject comprising the step of (a) obtaining genomic DNA from the human subject and (b) quantitating methylation in at least one target region selected from the group consisting of PLA2G16, CAV1, EVX1, MCF2L, FGF1, NCR2 and WNT2 and EXT1 and SPAG4 target, wherein significant methylation changes indicate the presence of prostate cancer or a prostate cancer field defect, wherein the change is relative to tissue from a second human subject who does not have prostate cancer. 1. A method of amplifying a target DNA sequence comprising the steps of:(a) providing a reaction mixture comprising a double-stranded bisulfite modified target DNA and (i) at least one pair of primers designed to amplify at least a portion of PLA2G16, wherein the primer pair comprises a first and a second primer that are complementary to the target DNA sequence, (ii) a polymerase and (iii) a plurality of free nucleotides comprising adenine, thymine, cytosine and guanine;(b) heating the reaction mixture to a first predetermined temperature for a first predetermined time to separate the strands of the target DNA from each other;(c) cooling the reaction mixture to a second predetermined temperature for a second predetermined time under conditions to allow the first and second primers to hybridize with their complementary sequences on the target DNA and to allow the polymerase to extend the primers; and(d) repeating steps (b) and (c) at least 10 times wherein an amplified target DNA sample is formed.2. The method of claim 1 , wherein the target DNA is from histologically normal prostate tissue of a subject.3. The method of wherein (iv) PCR reaction buffer and (v) MgCl2 are additionally added to step (a).4. The method of wherein the primers are methylated.5. The method of wherein the primers are not methylated.6. A method of selectively treating prostate cancer in a human subject comprising the steps of:(a) obtaining genomic ...

Methods for assaying palmitoyl protein thioesterase 1 and tripeptidyl peptidase activity in dried blood spots for detection of neuronal ceroid lipofuscinoses in newborns

The present disclosure provides assays for lysosomal enzymes, specifically palmitoyl protein thioesterase 1 (PPT1) and tripeptidyl peptidase 1 (TPP1), using, for example, tandem mass spectrometry. The assays involve the detection of enzymatic products obtained through the action of the lysosomal enzymes on new enzyme substrates, and can be used for quantitative enzyme activity measurements. The assays for the enzymes utilize a minimum steps for sample work up and can be run in a simplex format or in a duplex format for the detection of neuronal ceroid lipofuscinoses, or in a multiplex format with other mass spectrometry-based assays for screening of neuronal ceroid lipofuscinoses and other lysosomal storage disorders.

Fluorescent haloalkyl derivatives of reporter molecules well retained in cells

The subject invention provides a method for analyzing the metabolic activity in cells by improving the retention of a detectable reporter molecule only in intact cells where a particular enzyme is present. In particular, improved retention results from a two part process involving conjugation of haloalkyl-substituted derivatives of a reporter molecule with intracellular cysteine-containing peptides while unblocking the reporter molecule. The method for analyzing metabolic activity of cells involves the use of a substrate having the form XR-REPORTER-BLOCK wherein -BLOCK is a group selected to be removable by action of a specific analyte, to give REPORTER spectral properties different from those of the substrate, -REPORTER- is a molecule that, when no longer bound to BLOCK by a BLOCK-REPORTER bond, has spectral properities different from those of the substrate, and XR-- is a haloalkyl moiety that can covalently react with an intracellular thiol (Z--S--H) to form a thioether conjugate (Z--S--R--). After the substrate enters the cells, the analyte removes BLOCK to make REPORTER detectable by the change in spectral properties, and the haloalkyl XR reacts with the intracellular thiol to form the thioether conjugate inside the cells, which is well-retained in the cells.

Haloalkyl derivatives of reporter molecules used to analyze metabolic activity in cells

The subject invention provides substrates useful for analyzing the metabolic activity in cells by improving the retention of a detectable reporter molecule only in intact cells where a particular enzyme is present. In particular, improved retention results from a two part process involving conjugation of haloalkyl-substituted derivatives of a reporter molecule with intracellular cysteine-containing peptides while unblocking the reporter molecule. The substrates have the form XR-SPACER-REPORTER-BLOCK wherein -BLOCK is a group selected to be removable by action of a specific analyte, to give REPORTER spectral properties different from those of the substrate, -REPORTER- is a molecule that, when no longer bound to BLOCK by a BLOCK-REPORTER bond, has spectral properties different from those of the substrate, -SPACER- is a covalent linkage, and XR- is a haloalkyl moiety that can covalently react with an intracellular thiol (Z-S-H) to form a thioether conjugate (Z-S-R-). After the substrate enters the cells, the analyte removes BLOCK to make REPORTER detectable by the change in spectral properties, and the haloalkyl XR reacts with the intracellular thiol to form the thioether conjugate inside the cells, which is well-retained in the cells.

DEVICE TO INTENSIFY FLUORESCENCE AND KINETICS AND METHODS FOR USING THE DEVICE.

UN PORTADOR TENIENDO AL MENOS UN SOPORTE MEJORANDO LA ENERGIZACION Y FLUORESCENCIA Y UNA SUSTANCIA SECA SELECCIONADA DE ENTRE EL GRUPO COMPUESTO POR: SUSTRATOS FLUOROGENICOS, B-METILOLUMBERIFERONA, CUMARINA 7-AMINO-4 METILO, B-NAFTAFENILOAMINA, FLUORESCEINA, Y RESORCINOL DEPOSITADO SOBRE EL SOPORTE DEMOSTRANDO UNA MEJORA SUSTANCIAL DE LA ENERGIZACION Y FLUORESCENCIA DE SISTEMAS DE HIDROLISIS SOBRE LIQUIDOS. CUANDO EL DISPOSITIVO TIENE UNA PLURALIDAD DE SOPORTES Y LOS SOPORTES TIENEN DIFERENTES SUSTRATOS FLUOROGENICOS PUEDE DETERMINARSE EN LA SUSPENSION UN PERFIL DEL NIVEL DE REACCION DE UN ENCIMA DE UN MICRO ORGANISMO Y SE PUEDE USAR PARA IDENTIFICAR EL ORGANISMO. EL DISPOSITIVO TAMBIEN SE PUEDE USAR PARA CARACTERIZAR ENCIMAS EXPRESADOS POR OTROS ESPECIMENES BIOLOGICOS. A CARRIER HAVING AT LEAST ONE SUPPORT IMPROVING ENERGIZATION AND FLUORESCENCE AND A DRY SUBSTANCE SELECTED FROM AMONG THE GROUP COMPOSED BY: SUBSTRATES FLUOROGENIC, B-METHYLUMBERIFERONE, CUMARINA 7-AMINO-BORINA, BURIN-BORINA SUPPORT DEMONSTRATING A SUBSTANTIAL IMPROVEMENT OF THE ENERGIZATION AND FLUORESCENCE OF HYDROLYSIS SYSTEMS ON LIQUIDS. WHEN THE DEVICE HAS A PLURALITY OF SUPPORTS AND THE SUPPORTS HAVE DIFFERENT FLUOROGENIC SUBSTRATES, A PROFILE OF THE REACTION LEVEL OF A MICRO-ORGANISM ABOVE CAN BE DETERMINED TO IDENTIFY THE ORGAN. THE DEVICE CAN ALSO BE USED TO CHARACTERIZE TABLES EXPRESSED BY OTHER BIOLOGICAL SPECIMENS.

Assays for protease enzyme activity

Bioconjugates, kits and assays for detecting the activity of protease enzymes such as β-secretase and caspase enzymes are described. The bioconjugates include a tether having a segment capable of recognizing and interacting with (e.g., being cleaved by) the enzyme, a fluorescer including a plurality of fluorescent species conjugated to a first location on the tether, and a quencher conjugated to a second location on the tether. The segment capable of recognizing and interacting with the protease enzyme (e.g., β-secretase or caspase) is located between the first and second locations on the tether. The plurality of fluorescent species are associated with one another such that the quencher is capable of amplified super-quenching of the fluorescer. The assay is suitable for screening potential drugs for their efficiency in inhibiting the activity of protease enzymes such as β-secretase in a high throughput format where the potential drugs are evaluated.

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Dertermination of ions in fluids

내용 없음. No content.

Method of estimating activity of serine protease

Novel peptide derivatives which are acyl derivatives of luminol (5-amino-2,3-dihydro-1,4-phthalazinedione) or isoluminol (6-amino-2,3-dihydro-1,4-phthalazinedione) where the acyl residue is an amino acid or amino acid sequence with 2 to 4 amino acid residues, coupled with an amide bond, and where the alpha -amino group is either free or acylated, methods for their preparation and a method for laboratory diagnostics of proteases using the peptide derivatives. The derivatives are intended for quantitative determination of proteases or proteas-activity by release of luminol or isoluminol which in their free state can be brought to luminate intensely, but lose considerably in luminiscence when they are amide-bound to a peptide sequence.

Hemostasis assay

Method of assaying kallikrein formation substances

요약없음 No summary

Measurement of activity of angiotensinase

Novel compound for measuring alpha1-antitrypsin

(57)【要約】本公報は電子出願前の出願データであるた め要約のデータは記録されません。

Method and composition for determination of sodium ions in fluids

本发明涉及生物或非生物液体中的离子(下面称 为分析物)测定的方法和组合物。本发明的理论根据 是许多分析物有激活或抑制敏感酶的作用。分析物 可以是阳离子、阴离子、金属或非金属、单质或化合 物。在实践中，经常遇到分析物在样本中的浓度超过 相关分析指示酶的敏感性范围，或存在其他离子对酶 的敏感性产生干扰。本发明从多种途径提出并解决 这些问题的方案。

Aminoacetophenone derivatives and methods for measuring enzyme activity using the same

Test article and method for performing blood coagulation assays

A test article for determining coagulation capability in a blood sample comprises a porous membrane having a coagulation initiator and substrate impregnated therein. The pore dimensions and composition of the membrane may be selected so that only blood plasma can pass into the interior of the membrane, where coagulation is initiated. Alternatively, the substrate may be selected to have an emission and/or excitation wavelength which is not absorbed by hemoglobin. The substrate is activated by a component of the coagulation pathway, typically thrombin, and produces a detectable signal upon activation. By utilizing membrane matrix materials which are substantially free from interference with the coagulation pathway, accurate results can be achieved.

Method for measuring ions in liquid and composition therefor

Amino acid substituted-cresyl violet, synthetic fluorogenic substrates for the analysis of agents in individual in vivo cells or tissue

The present invention concerns a method to detect the presence of an enzyme in in vivo or in vitro tissue or cell, which method comprises: (a) obtaining a tissue or cell sample to be analyzed; (b) contacting the tissue or cell sample with a substrate of the structure selected from the group consisting of: X=H or one or more natural or synthetic amino acids with or without amino blocking groups, Y=H or one or more natural or synthetic amino acids with or without amino blocking groups, wherein X and Y are the same or different and are amino acid sequences of between about 1 to 1,000,000 amino acids wherein each amino acid is the same or a different amino acid, with the proviso that at least one of X or Y is at least one amino acid; (c) when an enzyme is present in the tissue or cell sample which degrades X, Y and combinations thereof, fluorescent cresyl violet is released in the tissue sample producing a color change; (d) detecting the presence and amount of the enzyme present by the detection and quantification of the fluorescence produced; and (e) optionally comparing the fluorescence to a pre-calibrated fluorescence scale to quantify the fluorescence present. A diagnostic kit for use and a method to prepare amino acid cresyl violet derivatives are described.

Method of preparing peptides or salts

Process for producing peptides or their salts

1488987 Tri- and tetrapeptides KABI AB 21 Nov 1975 [5 Dec 1974] 48019/75 Heading C3H A peptide of formula or a salt thereof, wherein R 1 is hydrogen, C 1 - C 12 alkanoyl, benzoyl, cyclohexylcarbonyl, substituted benzoyl, benzenesulphonyl or toluene sulphonyl; R 2 is nitrophenyl, naphthyl, nitronaphthyl, methoxynaphthayl, quinoyl or nitroquinoyl; A 1 is a direct bond or Gly, Ala, Val, Leu, Ile, Pro, Met, Phe or Tyr; A 2 is Glu, Gln, Asp, Asn. Peptides of the invention claimed are: The following intermediates are isolated: TETRAPEPTIDES: Cbo, Bz and H-Ile-Glu (OBzl)-Gly-Arg(NO 2 )-p-NA; and HBr.H-Ile-Glu- Gly-Arg(NO 2 )-pNA. TRIPEPTIDE: Boc - Gly(OBzl) - Gly - Arg (NO 2 )-pN A. The dipeptide isolated is Cbo-Gly-Arg(NO 2 )- pNA. The peptides are chromogenic substrates for serine proteases, and may be used for the determination of factor Xa in blood.

Protease detection sensor

본 발명은 특정 두 아미노산 사이를 절단하는 단백질분해효소 및 말단 아미노산을 절단하는 단백질분해효소를 이용한 단백질분해효소 검출용 센서에 관한 것이다. 본 발명에 따른 단백질분해효소 검출용 센서는 펩타이드 서열 안의 특정 두 아미노산 사이를 절단하는 목적 단백질분해효소, 및 N-말단 또는 C-말단 아미노산을 절단하는 단백질분해효소를 이용하여 제조됨으로써 색깔적, 형광적 또는 전기화학적 방법을 통해 목적 단백질분해효소를 고감도로 검출할 수 있는 효과를 나타낸다. The present invention relates to a protease for cleaving between two specific amino acids and a protease for detecting protease using a protease for cleaving the terminal amino acid. The sensor for detecting protease according to the present invention can be produced by using a target proteinase that cleaves between two specific amino acids in a peptide sequence and a protease that cleaves N-terminal or C-terminal amino acid, It exhibits an effect of detecting a target protein degrading enzyme with high sensitivity through an electrophoretic or electrochemical method.

Method for measuring enzyme activity

Method and composition for the determination of sodium ions in fluids

Method of potassium ion concentration assay in biological material

FIELD: medicine. SUBSTANCE: 10 mcl plasma or serum blood taken off in patient is placed to the incubation medium of the following composition: pyruvate kinase from Bacillus stearothermophillus (50-10000 U/l), phosphoenolpyruvate as neutral tris-salt (0.3-10 mmole/l), 4,7,13,16,21-pentaoxa-1,10-diazabicyclo-8,8,5-tricosane (up to 30 mmole/l), 50-500 mM buffer, pH 8 (0.10-0.8 mmole/l), manganese or magnesium ions (1-10 mmole/l), lithium chloride (2-100 mmole/l), ADF as free acid (0.5-10 mmole/l), serum lactate dehydrogenase (5000-100000 U/l), glutamic acid dehydrogenase (2500-20000 U/l, determined at 25 C), keto-glutaric acid as free acid (1-10 mmole/l) or glycerol dehydrogenase from Enterobacter aerogenes (50-1000 U/l), glycerol (0.3-3 mmole/l), 4,7,13,16,21-pentaoxa-1,10-diazabicyclo-8,8,5-tricosane (up to 30 mmole/l), NAD (0.1-5.0 mmole/l), buffer, pH 9 (20-500 mmole/l), serum albumin (up to 5 g/l), glutamic acid dehydrogenase (2500-20000 U/l, determined at 25 C), keto-glutaric acid as free acid (1-10 mmole/l), or acetaldehyde dehydrogenase from yeast (50-10000U/l), glycol aldehyde (0.3-30 mmole/l), 4,7,13,16,21-pentaoxa-1,10-diazabicyclo-88,5-tricosane (up to 30 mmole/l). NAD (0.05-2.0 mmole/l), buffer, pH 7-8 (50-500 mmole/l), dithiothreitol (0.1-2 mmole/l), serum albumin (up to 5 g/l), glutamic acid dehydrogenase (2500-20000 U/l, determined at 25 C), keto-glutaric acid as free acid (1-10 mmole/l), or acetaldehyde dehydrogenase (50-10000 U/l), 4-nitrophenyl acetate (0.3-30 mmole/l), 4,7,13,16,21-pentaoxa-1,10-diazabicyclo-8,8,5-tricosane (up to 30 mmole/l), NAD (0.001-0.1 mmole/l), buffer, pH 7-8 (50-500 mmole/l), dithiothreitol (0.1-2 mmole/l), serum albumin (up to 5 g/l), glutamic acid dehydrogenase (2500-20000 U/l, determined at 25 C), keto-glutaric acid as free acid (1-10 mmole/l). Then incubation mixture is incubated at 37 C for 0.1-5 min followed spectrophotometry at 340 nm and potassium ions measurement by calibration curve. EFFECT: improved method of ...

Measurement of number of microorganism

(57)【要約】本公報は電子出願前の出願データであるた め要約のデータは記録されません。

Method of detecting activity of x-prolyldipeptidylaminopeptidane

1518207 Determination of a prolyldipeptidylaminopeptidase AJINOMOTO Co. Inc. 29 Oct 1976 [30 Oct 1975 ] 45200/76 Heading G1B [Also in Divisions C2 and C3] A diagnostic reagent comprises a compound of Formula wherein X is an amino acid radical, YNH is the residue of YNH 2 wherein YNH 2 is selected from p-nitroaniline, p-phenylazoaniline, 4-phenylazo-1- naphthylamine; or an acid salt thereof, which compound may be porous. X is preferably the radical of an amino acid of up to 15 carbon atoms, most preferably selected from glycine, L-alanine, L-glutamic acid, L-aspartic acid, L-lysine and L-arginine, and the acid in the acid salt is preferably p-taluenesulphonic acid, hydrochloric acid or hydrobromic acid. A method of measurement of the activity of X-prolyldipeptidylaminopeptidase comprises contacting a compound of Formula X-Pro-NHY or an acid salt thereof with said X-prolyldipeptidylaminopeptidase in an aqueous medium at a pH of 6 to 9, preferably at 30‹C to 45‹C, and assaying the liberated YNH 2 . The process may be adapted to detect disease in a mammal (including homosapiens) by measurement of the YNH 2 liberated obtained by contacting serum which contains X-prolyldipeptidylaminopeptidase with a compound of Formula X-Pro-NHY, or an acid salt thereof, in an aqueous medium at 30‹C to 45‹C and at pH of 7À5 to 8À9. In the Examples, human serum and/or purified human submaxillary enzyme is assayed with glycylh-proline p-nitroanilide, L-hysyl-L-proline p-nitroanilide, L-alanyl-L-proline p-nitroaniline, L-glutamyl-L-proline p-nitroanilide, L-aspartyl-L- proline p-nitroanilide, glycyl-L-proline p-phenylazoanilide tosylate, glycyl-L-proline -nitroamilide tosylate. The liberated p-nitroaniline and p-phenylazoaniline are assayed spectrophatometrically.

Method of determining activity of serine proteases

Determination of ions in fluids

本发明涉及一种测定体液中钾离子的方法，其特征在于测定这些离子对微生物转移酶、微生物氧化还原酶、裂解酶或水解酶的活性的影响。本发明也涉及用于测定体液中钾离子的组合物，该组合物包括活性受钾离子影响的微生物转移酶或微生物氧化还原酶。

Improved new wound model

(57)【要約】 【課題】 慢性傷の治癒を研究し慢性傷の治療方法を評 価するための新しい有効なモデルと方法を提供する 【解決手段】 ストレプトゾトシンの注入により糖尿病 を豚に誘発する。コラゲナーゼとエラスターゼのレベル を糖尿病の豚の傷対非糖尿病の豚の傷で増やし、それに より慢性傷の状態をシミュレートする。

Kit for detecting infectious vaginitis and preparation method thereof

本发明提供一种检测感染性阴道炎的试剂盒。所述试剂盒包括干化学反应装置、样品稀释液和至少一种显色剂：其中反应装置具有至少一种检测以下指标的反应孔：过氧化氢、唾液酸苷酶、白细胞酯酶、β‑葡萄糖醛酸酶、凝固酶、乳酸、乙酰氨基葡萄糖苷酶、β‑内酰胺酶、脯氨酸氨肽酶、丙氨酸氨肽酶；样品稀释液中含有TritonX‑100和树胶；显色剂由固蓝B、固红B、固蓝BB、固蓝RR、固紫B或固红TR中的至少一种组成。本发明试剂盒产品可同时评估受检者生殖道微生态环境、清洁度和细菌性阴道病致病菌状，其操作简便、快速、成本低廉。

Fluorogenic protease substrates based on dye-dimerization

본 발명은 두 개의 형광 염료 기가 펩티드에 결합되어 있는 효소 기질을 준비하는 단계[상기 염료 기들은 염료 기의 형광을 실질적으로 자체 소광시키기에 충분히 근접 위치하며, 상기 염료 기 형광의 자체 소광은 염료 적층에 의해 일어남] 및 상기 펩티드를 효소적 분할시켜서 염료 적층에 의해 형성된 형광 염료 기를 방출시켜서 형광 세기를 증가시키는 단계를 포함하는 생물학적 분석법을 제공한다. 본 발명은 또한 본 발명의 방법에 사용되는 프로테아제 기질을 개시하고 있다. 본 발명은 미생물의 동정, 멸균 확인, 의약적 발견, 효소 분석, 면역 검증 및 기타의 생물학적 분석에서의 용도를 밝히고 있다. The present invention provides a method of preparing an enzyme substrate having two fluorescent dye groups bonded to a peptide, wherein the dye groups are positioned close enough to substantially self-quench the fluorescence of the dye group, and the self-quenching of the dye group fluorescence And enzymatic cleavage of the peptide to release fluorescent dye groups formed by dye deposition to increase fluorescence intensity. The invention also discloses protease substrates for use in the methods of the invention. The present invention finds use in the identification of microorganisms, sterilization confirmation, medical discovery, enzyme analysis, immunoassay and other biological assays.

Method of producing tripeptides or salts thereof

Patent FR2293439B1

Method for determination of pyrogen content

Abstract of the disclosure: METHOD FOR DETERMINATION OF PYROGEN CONTENT A method for determination of a pyrogen content by using a centrifugation type filtration unit for centrifugal filtration is disclosed. A sepcimen is brough into contact with an adsorbent having pyrogen absorbability in the filtration unit and any non-adsorbed material is separated and removed by centrifugation so that a pyrogen is specifically adsorbed by the adsorbent and then the pyrogen adsorbed on the adsorbent is reacted with a detection reagent to determine the pyrogen content.

METHOD FOR DETERMINING THE ACTIVITY OF THE ENZYME TRANSFORMING ANGIOTENSIN

PROCEDE POUR DETERMINER L'ACTIVITE DE L'ENZYME TRANSFORMANT L'ANGIOTENSINE IL CONSISTE A EFFECTUER LES STADES 1 MELANGER UN LIQUIDE CONTENANT L'ENZYME TRANSFORMANT L'ANGIOTENSINE A UN REACTIF CONSISTANT ESSENTIELLEMENT EN X-HIPPURYL-L-HISTIDYL-L-LEUCINE AYANT LA FORMULE SUIVANTE, EN HIPPURICASE, EN PEROXYDASE, EN 4-AMINOANTIPYRINE ET EN HO, ET 2 MESURER COLORIMETRIQUEMENT LA CONCENTRATION DU COLORANT QUINONIMIQUE PREPARE AU STADE 1: (CF DESSIN DANS BOPI) DANS LAQUELLE X REPRESENTE OH, NH OU N(CH). MEDECINE. PROCESS FOR DETERMINING THE ACTIVITY OF THE ENZYME TRANSFORMING ANGIOTENSIN IT CONSISTS OF PERFORMING STAGES 1 MIXING A LIQUID CONTAINING THE ENZYME TRANSFORMING ANGIOTENSIN TO A REAGENT CONSISTING OF ESSENTIALLY X-HIPPURYL-L-L-HISTIDYL-HISTIDYL THE FOLLOWING FORMULA, IN HIPPURICASE, PEROXIDASE, 4-AMINOANTIPYRINE AND HO, AND 2 MEASURE COLORIMETRICALLY THE CONCENTRATION OF QUINONIMIC DYE PREPARED IN STAGE 1: (CF DRAWING IN BOPI) IN WHICH X N (OH) OR NH REPRESENTS, NH, . MEDICINE.

NOVEL ENZYMATIC SUBSTRATES FOR THE DETECTION OF PSEUDOMONAS AERUGINOSA, COMPOSITIONS CONTAINING SAME, AND METHOD FOR DETECTING SUCH SPECIES

METHOD FOR EVIDENCE OF ENZYMATIC ACTIVITY OF MICROORGANISMS

The method consists in the use of one compound of formula: X-NH-R in which X represents one 5-bromoindole-3-yle group and R represents the acyl radical of one amino acid selected between leucine and alanine, as tracer for demonstrating, by the formation of a coloured product, a peptidase activity in a culture of micro-organisms.

NEW CHROMOGENIC ENZYMATIC SUBSTRATES

Patent FR2183188A1

NEW ENZYME CHROMOGENOUS SUBSTRATES

METHOD FOR EVIDENCE OF AN ENZYMATIC ACTIVITY OF MICROORGANISMS

Assays and devices for the detection of extrahepatic biliary atresia

The present invention involves a variety of assay methods end devices for screening or diagnosing the occurrence of extrahepatic biliary atresia. In particular, the methods and devices involve the detection of dipeptidyl peptidase IV in a test sample as indicative of extrahepatic biliary atresia.

Patent FR2455083B1

METHOD FOR DETERMINING THE ACTIVITY OF THE ANGIOTENSIN-TRANSFORMING ENZYME

NOVEL AMIDE USABLE AS SYNTHETIC SUBSTRATE AND DOSING METHOD USING SAME

LA PRESENTE INVENTION CONCERNE UN PROCEDE DE DOSAGE D'UNE ACTIVITE ENZYMATIQUE COMPRENANT LE TRAITEMENT D'UNE AMINE DE FORMULE: (CF DESSIN DANS BOPI) DANS LAQUELLE R EST UN RADICAL L-LEUCYLE OU G-L-GLUTAMYLE, R, R, R, R ET R SONT UN ATOME D'HYDROGENE OU D'HALOGENE OU UN RADICAL ALKYLE INFERIEUR, ALCOXY INFERIEUR, AMINO, AMINO SUBSTITUE, HYDROXY, CARBOXY OU SULFO, ET R ET R PEUVENT CONSTITUER ENSEMBLE UN CYCLE CARBONE, OU UN SEL SOLUBLE DANS L'EAU CORRESPONDANT, AVEC UNE PEPTIDASE, LE TRAITEMENT DE L'AMINE AINSI LIBEREE, AVEC UNE OXYDASE QUI CONSOMME DE L'OXYGENE ET FORME UN COLORANT EN PRESENCE D'UN COUPLEUR PUIS LA MESURE QUANTITATIVE DES CHANGEMENTS DETECTABLES. THE PRESENT INVENTION CONCERNS A METHOD FOR ASSESSING AN ENZYMATIC ACTIVITY INCLUDING THE TREATMENT OF AN AMINE OF FORMULA: (CF DRAWING IN BOPI) IN WHICH R IS A RADICAL L-LEUCYL OR GL-GLUTAMYL, R, R, R, R AND R ARE A HYDROGEN OR HALOGEN ATOM OR A LOWER RADICAL ALKYL, LOWER ALCOXY, AMINO, SUBSTITUTE AMINO, HYDROXY, CARBOXY OR SULFO, AND R AND R CAN CONSTITUTE A SOLUB CARBON CYCLE, OR SULFO, TOGETHER. WATER CORRESPONDING, WITH A PEPTIDASE, THE TREATMENT OF THE AMINE THUS RELEASED, WITH AN OXIDASE WHICH CONSUMES OXYGEN AND FORMED A COLOR IN THE PRESENCE OF A COUPLER THEN THE QUANTITATIVE MEASUREMENT OF DETECTABLE CHANGES.

NOVEL PEPTIDES CARRYING A FLUOROPHORE, PROCESS FOR THEIR PREPARATION AND THEIR APPLICATION TO FLUORIMETRIC DETERMINATION OF ENDOTOXINS

PEPTIDES, UTILISABLES POUR LE DOSAGE FLUORIMETRIQUE DES ENDOTOXINES, REPONDANT A LA FORMULE GENERALE: (CF DESSIN DANS BOPI) DANS LAQUELLE PEPT- DESIGNE

Identifying microorganisms by measuring enzymatic activity in the presence of enzyme activity affecting agents

A method for rapidly identifying microorganisms by determining the rates of enzymatic hydrolysis of a plurality of substrates in the presence of at least one enzyme activity affecting agent, called an "affector" is provided. The substrates are selected from fluorogenic and chromogenic substrates to create a characteristic pattern of enzymatic cleavage rates by enzymes expressed by the unidentified microorganism. This characteristic pattern of enzymatic cleavage rates is a "fingerprint" of the unidentified microorganism when in the presence of the affector. The pattern of enzymatic cleavage rates for the unidentified microorganism is compared to a pattern of enzymatic cleavage rates of the same substrates in the presence of the same affector for one or more identified classes or subclasses of microorganisms. The unidentified microorganism is then identified as belonging to a class or subclasses of the known microorganisms which most closely matches the pattern of enzymatic cleavage rates in the presence of the affector.

Patent FR2183170A1

ENZYMATIC DETERMINATION PROCESS

Immunosorbent-amidolytic method for detecting human urinary plasminogenactivator precursor (pro-upa) and human urinary plasminogen activator (u-pa)

ABSTRACT The present invention is directed to a method of selecti-ve assay of urinary plasminogen activator zymogen (pro-uPA) (commonly known also as pro-urokinase) and urinary plasminogen activator (u-PA) (commonly known also as urokinase) in biological fluids as well as in any kind of solution containing them, either separately or jointly. One feature of this method is in fact that it allows the determination of pro-uPA also in the presence of its enzymatically active derivative u-PA.

Electrochemical protease or anti-protease determn. - by amperometric determn. of amine released from peptide amide substrate

Determn. of protease or antiprotease enzymes is carried out by (a) contacting the enzyme is an aq. medium with a substrate of formula A-B (where A is a peptide residue in which the terminal N atom is opt. substd. and the C-terminal aminoacid is arginine, or A is N-substd. arginyl, and B is the residue of an electrochemically oxidisable or reducible amine H-B), and (b) determining the released amine by amperometry. The method is esp. useful for determn. of enzymes involved in the blood clotting system or complement. It is simple, accurate and reliable, and can be applied to both homogeneous and heterogeneous media.

PROCESS FOR DETERMINING CATHEPSIN B IN THE PRESENCE OF OTHER PROTEOLYTIC ENZYMES AND COMPOUNDS USEFUL THEREFOR

L'INVENTION A POUR OBJET UN PROCEDE PERMETTANT DE DETERMINER LA CATHEPSINE B EN PRESENCE D'AUTRES ENZYMES PROTEOLYTIQUES ET DES COMPOSES UTILES A CET EFFET. LE PROBLEME A RESOUDRE CONSISTE A FOURNIR UN SUBSTRAT HAUTEMENT SPECIFIQUE DE LA CATHEPSINE B, INDEPENDAMMENT DE LA PRESENCE DE TRYPSINE ET D'ENZYMES PROTEOLYTIQUES ANALOGUES. CE PROCEDE CONSISTE D'UNE PART A MELANGER UN ECHANTILLON DESDITS FLUIDES AVEC UN SUBSTRAT ET SES SELS D'ACIDE DE FORMULE Z - R - R - X DANS LAQUELLE X EST UN FRAGMENT DE MOLECULE INDICATEUR LIBERE PAR COUPURE DE LA LIAISON R-X PAR LA CATHEPSINE B ET EST DETECTABLE LORS DE LA COUPURE, R EST UN GROUPE AMINO-ACIDE AYANT LA CONFIGURATION L AU CARBONE EN ALPHA DU GROUPE CARBONYLE ET N'EST PAR CHARGE POSITIVEMENT DANS L'INTERVALLE DE PH AUQUEL S'EFFECTUE LE DOSAGE, R EST UN GROUPE AMINO-ACIDE HYDROPHOBE AYANT LA CONFIGURATION L AU CARBONE EN ALPHA DU GROUPE CARBONYLE, ET Z EST UN GROUPE DE BLOCAGE AMINO N'INTERFERANT PAS AVEC LA LIAISON SELECTIVE DE LA CATHEPSINE B AVEC LES GROUPES R ET R, LEDIT MELANGE ETANT REALISE DANS UN MILIEU AQUEUX AYANT UN PH COMPRIS DANS UN INTERVALLE POUR LEQUEL LA CATHEPSINE B EST ACTIVE, ET LE MELANGE AYANT UNE CONCENTRATION EN SUBSTRAT NOTABLEMENT PLUS GRANDE QUE LA CONCENTRATION EN CATHEPSINE B, ET SUFFISANTE POUR QUE LE GROUPE X COUPE PUISSE ETRE DETECTABLE, ET D'AUTRE PART A MESURER LA VITESSE AVEC LAQUELLE LE GROUPE X EST COUPE DU SUBSTRAT. L'INVENTION TROUVE UNE APPLICATION AVANTAGEUSE POUR LE DIAGNOSTIC DES MALADIES METASTATIQUES. THE SUBJECT OF THE INVENTION IS A PROCESS FOR DETERMINING CATHEPSIN B IN THE PRESENCE OF OTHER PROTEOLYTIC ENZYMES AND COMPOUNDS USEFUL THEREFOR. THE PROBLEM TO BE SOLVED IS TO PROVIDE A HIGHLY SPECIFIC CATHEPSIN B SUBSTRATE, INDEPENDENT OF THE PRESENCE OF TRYPSIN AND SIMILAR PROTEOLYTIC ENZYMES. THIS PROCESS CONSISTS ON THE ONE HAND OF MIXING A SAMPLE OF THE SAID FLUIDS WITH A SUBSTRATE AND ITS SALTS OF ACID OF FORMULA Z - R - R - X IN ...

Kinetic assay for endotoxin using limulus amebocyte lysate and chromogenic substrate

A kinetic assay procedure is provided which permits measurement of endotoxin concentration in the range from 0.005 EU/ml to 50 EU/ml. The assay procedure relies on a single reagent substrate composition comprising Limulus amebocyte lysate and a chromogenic substrate. This assay procedure is easily automated and it provides substantial improvement in both range and sensitivity over previously available endotoxin assays.

Patent FR2497798B1

Diagnostic method

Disclosed is a method useful in the differential diagnosis of colon cancer or HIV infection. Persons suffering from colon cancer or infected with HIV have increased levels of extracellular prosomes in their blood in comparison to the blood of persons not suffering from these diseases. The presence and quantity of these extracellular prosomes can be detected either with certain labelled anti-prosomal protein monoclonal antibodies or by measuring the amount of protease activity in an extracted portion of blood which would contain the extracellular prosomes. The results once obtained can be compared with a ''norm'' derived from a person not suffering from such diseases.

Patent FR2372798B1

Hemostasis assay

The invention relates to a hemostasis assay comprising the provision of a reaction mixture comprising a blood product to be tested, a trigger molecule for inducing thrombin generation, a thrombin-specific substrate that upon cleavage by thrombin produces a measurable thrombin-specific signal, a trigger molecule for inducing plasmin generation, a plasmin-specific substrate that upon cleavage by plasmin produces a measurable plasmin-specific signal, a phospholipid-containing surface and calcium ions, and determination of the amount of thrombin and the amount of plasmin generated in the reaction mixture in time starting at t=0 by measuring the thrombin-specific and plasmin-specific signals.

USE OF CHROMOGENIC SUBSTRATES IN THE DETERMINATION OF CANDIDA.

La présente invention a trait à une nouvelle utilisation d'un substrat chromogène pour la détermination de souches de Candida et de souches apparentées appartenant à l'ensemble des Torulopsis, ladite utilisation étant caractérisée en ce que ledit substrat chromogène est choisi parmi l'ensemble comprenant les substrats chromogènes sensibles aux aminoamidases ou aminopeptidases. Elle concerne également un procédé d'identification desdites souches ainsi que le nécessaire d'identification renfermant au moins un desdits substrats chromogènes. Pour identifier spécifiquement les souches de Candida albicans, on préconise de faire appel à un substrat choisi parmi H-L-Pro-pNA et ses sels d'addition.

DIPEPTIDES, PROCESS FOR THE PREPARATION AND USE IN THE ASSAYING OF PROTEASES

LA PRESENTE INVENTION VISE EN TANT QUE PRODUITS INDUSTRIELS NOUVEAUX LES DIPEPTIDES DE FORMULE : Q-A-A-R OU Q EST UN RESTE RO-CO-(CRR)N -CO (OU R EST H, ALKYLE EN C1-C4, PHENYLE EVENTUELLEMENT SUBSTITUE, BENZYLE EVENTUELLEMENT SUBSTITUE OU P-CHCHSOCH, R ET R IDENTIQUES OU DIFFERENTS REPRESENTENT CHACUN H OU ALKYLE EN C-C, ET N EST UN NOMBRE ENTIER VALANT 1 A 5), A EST UN RESTE D'AMINOACIDE NON BASIQUE, A EST UN RESTE D'A-AMINOACIDE BASIQUE, ET R EST UN RESTE AMINO NHR CONSTITUANT UN MARQUEUR CLIVABLE DE A PAR HYDROLYSE ENZYMATIQUE (OU R EST UN SUPPORT DU MOYEN DE MARQUAGE); ET LEURS SELS D'ADDITION. CES NOUVEAUX PRODUITS SONT UTILES COMME SUBSTRATS ENZYMATIQUES NOTAMMENT DANS LE DOMAINE DES DOSAGES BIOLOGIQUES. THE PRESENT INVENTION AIMS AS NEW INDUSTRIAL PRODUCTS AT DIPEPTIDES OF FORMULA: QAAR OR Q IS A REST RO-CO- (CRR) N -CO (OR R IS H, ALKYL IN C1-C4, PHENYL POSSIBLE SUBSTITUTE, BENZYL POSSIBLE SUBSTITUTE OR IDENTICAL OR DIFFERENT P-CHCHSOCH, R AND R EACH REPRESENTS H OR ALKYL IN CC, AND N IS A WHOLE NUMBER OF 1 TO 5), A IS A REMAINDER OF NON-BASIC AMINOACID, A IS A REMAINDER OF A-AMINOACID BASIC, AND R IS AN AMINO NHR REMAINDER CONSTITUTING A MARKER CLIVABLE FROM A BY ENZYMATIC HYDROLYSIS (OR R IS A SUPPORT OF THE LABELING MEDIA); AND THEIR ADDITIONAL SALTS. THESE NEW PRODUCTS ARE USEFUL AS ENZYMATIC SUBSTRATES, ESPECIALLY IN THE FIELD OF BIOLOGICAL ASSESSMENTS.

Method of enzymatic determination

For the determination of a compound of formula: in which R1 is a hydroxyl or amino group, or hydrogen if at least one of the substituents R2, R3, R4, R5 and R6 is a hydroxyl or amino group, and R2, R3, R4, R5 and R6 are chosen from hydrogen, halogens and lower alkyl, lower alkoxy, amino, substituted amino, hydroxyl, carboxyl or sulpho groups, or R5 and R6 together form a ring, a reaction system is established containing the compound to be determined and a coupling agent and an enzyme capable of consuming oxygen and of producing a pigment in the presence of the compound and the coupling agent. A detectable change in the reaction system is measured in order to determine the compound in question. Application especially to the determination of hydrolases.

WATER-SOLUBLE COUMARIN DERIVATIVES, THEIR PREPARATION AND THEIR USE AS ENZYME SUBSTRATE.

Hydrophobic aminocoumarin derivatives, and their use as substrates for proteolytic enzymes or for the preparation of such substrates.

L'invention concerne un dérivé d'aminocoumarine de formule: (CF DESSIN DANS BOPI) dans laquelle R1 est un groupe alkyle, cycloalkyle ou aryle, éventuellement substitué, l'un des R2 à R5 est un groupe amino de formule NH2 , NHR7 , NH-COOR7 , N(R8 )COOR7 , NHR9 ou NR7 R9 , et les autres R2 à R5 ainsi que R6 sont des atomes d'hydrogène ou d'autres substituants. Ces dérivés d'aminocoumarine sont utilisables comme substrat d'enzyme ou pour la synthèse de substrats d'enzyme, adaptés à la détection d'enzymes sur des supports solides en contact avec un milieu aqueux, en milieu hétérogène. The invention relates to an aminocoumarin derivative of formula: (CF DRAWING IN BOPI) in which R1 is an alkyl, cycloalkyl or aryl group, optionally substituted, one of R2 to R5 is an amino group of formula NH2, NHR7, NH-COOR7, N (R8) COOR7, NHR9 or NR7 R9, and the other R2 to R5 as well as R6 are hydrogen atoms or other substituents. These aminocoumarin derivatives can be used as enzyme substrate or for the synthesis of enzyme substrates, suitable for the detection of enzymes on solid supports in contact with an aqueous medium, in a heterogeneous medium.

Peptide compounds and their use as protease substrates

本発明は、一般にペプチド化合物及び塩、特に、マトリックスメタロプロテア−ゼ（“ＭＭＰ”）基質のようなプロテア−ゼ基質として有用なペプチド化合物及び塩に向けられている。本発明はまた、そのような化合物及び塩の製造方法と、例えばそのような製造方法に使用してもよいアミノ酸に向けられている。本発明は、更に、そのような化合物及び塩を、例えば潜在的なプロテア−ゼ阻害剤の効力の評価、及びプロテア−ゼ活性に関連する疾患の検出又はモニタ−に使用する方法に向けられている。

Immunadsorbic amidolitic method for indicating plasminogene activator precursor /pro-u-pa/ and plasminogene activator /u-pa/ of human urine

Diagnostic assay method for the detection of oral pathogenic bacteria mixtures

1. Diagnostic procedure for detecting a mixture of pathogenic oral plaque bacteria associated with gingivitis and parodontitis, characterized in that an oral plaque specimen is collected in a sterile, small glass bottle containing 0.5 - 1 ml of HEPES buffer or reduced transport liquid and from 5 - 10 cleaned, sterile glass beads having a diameter of from 2 - 3 mm, and that the small bottle is thoroughly shaken for about 10 sec., the contents are divided up into from 4 - 8 parts of 100 mu l each, and each part is tested for enzymatic activity by mixing each part specimen with a chromogenic substrate and incubating it, the substrates being chosen from the group of the following substrates : N-alpha-benzoyl-D,L-arginine-beta-naphthylamide.HCl ; L-valine-beta-naphthylamide ; L-leucine-beta-naphthylamide.HCl ; L-pyrrolidonyl-beta-naphthylamide ; L-serine-beta-naphthylamide ; L-arginine-beta-naphthylamide ; L-alamine-beta-naphthylamide ; L-phenylalanine-beta-naphthylamide ; L-hydroxy-proline-beta-naphthylamide and glycylglycyl-beta-naphthylamide, which are substrates of enzymes that are released by pathogenic bacteria contained in the mixture to be detected, the positive enzymatic reaction being detected by means of attacked substrates which, through the addition of chromogenic reagents, have modified light-absorption values, and the substantially positive enzymatic reaction indicates the presence of a pathogenic bacterial mixture.

Method and composition for the detection of sodium ions in liquids

Endotoxin kinetic assay using Limulus amoebocyte lysate and chromogenic substrate

Method of producing tripeptides

Easily split enzyme substrates for the quantification of proteases having the general formula wherein R 1 = H or a protective group, preferably t-butyl-oxycarbonyl, benzyloxycarbonyl; A, - Gly, Ala, Val, Leu, Ile. Ser, Thr, Pro, Pip, Phe or Tyr; A 2 - Arg or Lys; R 2 = an aromatic, possibly substituted, hydrocarbon group, wherein -NH-R 2 is a physico-chemically determinable group, preferably a chromogenic or fluorogenic group which is split by a present enzyme and then forms a cleavage product of the formula H 2 N - R 2 the amount of which can be quantified. Process for the production of said substrates. Method in the laboratory diagnostics of proteases using said substrates.

Arginyl-3-carboxy-4-hydroxyanilide

(57)【要約】本公報は電子出願前の出願データであるた め要約のデータは記録されません。

Process for preparing specific chromogen new tetrapeptide derivatives as enzyme-substrates

Patent NO135362C

Method for detecting thrombin,plasmin,tripsin and thrombin-like enzymes in biological fluids

A substrate for the quantitative determination of enzymes in human and mammal body fluids as well as in animal cell extracts and glandular venoms of cold-blooded animals, which has the structure R1 - Gly - Pro - X - NH - R2 wherein R1 represents hydrogen or a blocking acyl or sulfonyl group, R2 represents an aromatic hydrocarbon group which may carry substituents and X represents arginyl or lysyl, -NH-R2 being a chromogenic or fluorescent group capable of yielding a split product NH2-R2 the quantity of which can be measured by photometric, spectrophotometric or fluorescence-photometric methods.

Method for detecting endotoxin using lyglycos amobotassium lysate substantially free of coagulogen

본 발명은 발색 분석을 이용하여 샘플에서 내독소를 검출하는 방법에 관한 것으로, 이 방법은: (a) 샘플을 리물루스 아메보사이트 라이세이트 (LAL) 및 발색 기질을 포함하는 시약과 접촉시키는 단계; 및 (b) 샘플에서 내독소의 존재하에 발색 기질의 변화로부터 기인하는 발색 효과를 측정하는 단계를 포함하고, LAL은 실질적으로 코아굴로겐이 없다. 본 발명은 또한 실질적으로 코아굴로겐이 없는 LAL을 포함하는 조성물과 키트, 및 그의 제조방법에 관한 것이다.

Reagent for the optical determination of the blood coagulation behaviour

ABSTRACT The present invention provides a reagent for the optical determination of blood coagulation behaviour (Quick test), comprising thromboplastin, a synthetic thrombin substrate and a buffer, characterised by a content of non-proteolytically active thromboplastin.

PROCEDURE FOR DETERMINING FLUIDS IONES.

Use of indolamine derivatives for detecting micro-organism peptidase

Compounds of formula X-NH-R, in which X represents an optionally substituted indol-3-yl group and R represents the acyl residue of an amino acid or of a peptide, enabling the detection of peptidase activity in a micro-organism culture medium, including a gelled medium, by forming a stain or fluorescence in the medium.

Process for the quantitative determination of the blood clotting factor XII in human plasma.

A method for assaying blood coagulation factor XII in human blood plasma wherein plasma is treated with an activator in order to convert factor XII present in the plasma into factor XIIa, the latter is reacted with a tripeptide derivative which is split by the enzymatic action of factor XIIa and forms a colored or fluorescent split product, and the quantity of this split product is measured photometrically, spectrophotometrically or fluorescence-spectrophotometrically.

REAGENT FOR OPTICAL DETERMINATION OF THE BLOOD COGULATION CONDITION.

Reagens for optisk bestemmelse av blodkoaguleringsforholdet (Quick-test) inneholder et syntetisk trombinsubstrat, buffer og ikke proteolytisk aktivt tromboplastin. Et ikke proteolytisk aktivt tromboplastin oppnås ved fremstilling av et acetontørrpulver fra hjerne, inkubasjon av en nøytral, vandig løsning av acetontørr-pulveret ved 25 til 40°C, utvinning av den uløselige fraksjon, behandling av en suspensjon av denne fraksjon i fortynnet saltløsning med et overflateaktivt middel i nærvær av formiat og tørking av den fraskilte, løse-lige fraksjon.

METHOD FOR PRODUCING NEW PEPTIDES SUITABLE AS SPECIFIC CHROMOGENIC ENZYME SUBSTRATES FOR SERINE PROTEASES

Patent FR2465785B1

Method and composition for the detection of sodium ions in liquids

Patent JPS6356501B2

METHOD FOR DETECTING THE ENCYMACTIVITY OF MICROORGANISMS

Patent JPH0563158B2

Method of detecting an endotoxin using limulus amebocyte lysate substantially free of coagulogen

USE OF TRIPEPTIDE DERIVATIVES FOR THE QUANTITATIVE DETERMINATION OF PLASMINOGEN ACTIVATORS.

Patent JPS4940192A

NEW CHROMOGENA ENZYME SUBSTRATE FOR SERINE PROTEASES

System for diagnosing periodontal disease

A colorimetric assay system for diagnosing periodontal disease utilizes a chromogenic test substance for measuring proteolytic activity in a specimen which may contain suspected periodontopathogenic bacteria. The colorimetric assay method of the present invention operates to detect the presence of proteolytic activity in a specimen of subgingival plaque, for example. A chromogenic test substance comprises a peptide substrate which is hydrolyzable by proteolytic enzymes in the plaque specimen to release the chromophore. Detection of a color change in the test substance indicates whether such proteolytic activity is present. In specific illustrative embodiment, the chromogenic test substance comprises N-benzoyl-DL-arginine-2-naphthylamide (BANA) or benzoyl-DL-arginine-p-nitroanilide (BAPNA). In the case of BANA, for example, the chromophore, .beta.-naphthylamide, is detected by the addition of a color developer, such as fast garnet. The development of a red-orange color is interpreted to indicate the presence of periodontal disease associated with anaerobic periodontopathogens, such as B. gingivalis), T. denticola, and B. forsythus, and the development of a yellow color is interpreted to indicate the absence of periodontal disease.

Method for the detection of plasminogen activators, their inhibitors or stimulators

Composition for detection of at least one strain and/or species of microorganisms and process for detecting the bacterial species pseudomonas aeruginosa

Patent FR2197470A5

Test system for the determination of proteases, active in-vivo in haemostasis, in biological fluids

Determining in vivo active proteases (I) of hemostasis or trypsin and subtilisin in a biological fluid, comprising incubating the test sample with at least one chromogenic or fluorogenic substrate (A) for the appropriate enzyme, and optional additives, is new. Independent claims are also included for the following: (1) determining the contact phase capacity (CPC) of a biological fluid by treatment with at least one substrate (A') for at least one hemostasis enzyme, at least one contact phase activator (B) and optionally other additives; and (2) test system for the new processes comprising (A) and optionally other additives and auxiliaries.

New chromogenic enzyme substrates

Method and apparatus for diagnosing intracellular parasite infections using an enzyme detection system

METHOD AND APPARATUS FOR DIAGNOSING INTRACELLULAR PARASITE INFECTIONS USING AN ENZYME DETECTION SYSTEM Abstract of the Disclosure The present invention involves a highly specific chemical system for detecting parasite-infected cells. The method is especially effective in detecting intraerythrocytic diseases, especially malaria. With respect to malaria, chemical agents are used to detect enzymes produced by the infecting parasites. Blood samples are combined with a plurality of substrates which are subject to enzymatic hydrolysis. Hydrolysis is rapid and may be detected in two ways. The first method involves substrates having a fluorescent detecting group. Upon hydrolysis, the fluorescent group is cleaved and detected using a conventional fluorescent light source. Alternatively, substrates may be used having a detecting group which forms a visibly colored material when combined with a secondary reagent. These techniques produce a unique colored or fluorescent pattern which enables the rapid and accurate determination of parasite infection. Furthermore, parasite diagnosis is accomplished without the use of expensive and complex diagnostic equipment.

METHOD FOR DETERMINING CATHEPSIN B IN THE PRESENCE OF OTHER PROTEOLYTIC ENZYMES, AND COMPOUNDS USEFUL FOR THIS.

Patent JPS5183595A

Composition and test device for determining the presence of leukocytes, containing a zwitterion coupling agent

ABSTRACT OF THE DISCLOSURE A composition and test device for determining the presence of an analyte selected from leukocytes, esterase and protease in a test sample. The composi-tion comprises an ester capable of producing a de-tectable response upon interaction with said analyte, and a diazonium salt having the structure