Academic literature on the topic 'Chromogenic substrates'

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Journal articles on the topic "Chromogenic substrates"

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Hutton, R. A. "Chromogenic substrates in haemostasis." Blood Reviews 1, no. 3 (1987): 201–6. http://dx.doi.org/10.1016/0268-960x(87)90036-1.

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Burrous, Mary R., and John Westley. "Chromogenic substrates for sulfurtransferases." Analytical Biochemistry 149, no. 1 (1985): 66–71. http://dx.doi.org/10.1016/0003-2697(85)90477-4.

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Hortin, Glen L., Ilka Warshawsky, and Maryline Laude-Sharp. "Macromolecular Chromogenic Substrates for Measuring Proteinase Activity." Clinical Chemistry 47, no. 2 (2001): 215–22. http://dx.doi.org/10.1093/clinchem/47.2.215.

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Abstract Background: Proteinase activities are often measured using chromogenic substrates that are much smaller than physiological substrates. Methods: The hydrodynamic size of macromolecular substrates (macrosubstrates) prepared by linking small chromogenic substrates to polyethylene glycol was determined by gel filtration. Efficiency of macrosubstrate cleavage by proteinases and α2-macroglobulin-proteinase complexes was monitored spectrophotometrically. Results: Macrosubstrates had hydrodynamic radii of ∼20 Å, similar to proteins with a molecular weight of 18 000. Different macrosubstrates
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Johnson, Gary M., and Robert Schaeper. "Chromogenic Lactate−Leukocyte Esterase Substrates." Bioconjugate Chemistry 8, no. 1 (1997): 76–80. http://dx.doi.org/10.1021/bc960081h.

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Marmuse, Laurence, Michèle Asther, David Navarro, et al. "Chromogenic substrates for feruloyl esterases." Carbohydrate Research 342, no. 15 (2007): 2316–21. http://dx.doi.org/10.1016/j.carres.2007.06.004.

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Conyers, Susan M., and David A. Kidwell. "Chromogenic substrates for horseradish peroxidase." Analytical Biochemistry 192, no. 1 (1991): 207–11. http://dx.doi.org/10.1016/0003-2697(91)90208-b.

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Marmuse, Laurence, Michèle Asther, Emeline Fabre, et al. "New chromogenic substrates for feruloyl esterases." Organic & Biomolecular Chemistry 6, no. 7 (2008): 1208. http://dx.doi.org/10.1039/b717742a.

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Somorin, O., W. Okiei, T. Emokpae, and M. Ogunlesi. "New lysine chromogenic substrates for trypsin." International Journal of Biological Macromolecules 9, no. 1 (1987): 27–31. http://dx.doi.org/10.1016/0141-8130(87)90021-3.

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Bozic, Natasa, Biljana Dojnov, Aleksandra Milovanovic, Vera Nenadovic, Jelisaveta Ivanovic, and Z. Vujcic. "Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae." Archives of Biological Sciences 60, no. 3 (2008): 403–9. http://dx.doi.org/10.2298/abs0803403b.

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Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific
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Mašková, Hana P., George Kokotos, Chryssa Tzougraki, and Tomislav Barth. "Synthesis and use of an aminoquinolinone derivative for the fluorometric determination of oxytocinase." Collection of Czechoslovak Chemical Communications 54, no. 10 (1989): 2802–8. http://dx.doi.org/10.1135/cccc19892802.

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A new fluorogenic substrate for the determination of the activity of human serum oxytocinase-cystine aminopeptidase (EC 3.4.11.3), H-Cys(Bzl)-NH-Meq, has been synthesized. The affinity of H-Cys(Bzl)-NH-Meq to oxytocinase was by two orders higher than that of the usually employed chromogenic substrates. The Michaelis constant of oxytocinase for this substrate was within the range of the optimum pH (7.0–7.5) 2.3.10-6 mol l-1, i.e. in the region of the affinity of the natural substrate, oxytocin. The concentration of dimethylsulfoxide used for the solubilization of H-Cys(Byl)-NH-Meq (<0.4%) di
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Dissertations / Theses on the topic "Chromogenic substrates"

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Davidson, Gwen. "The development of chromogenic substrates for microbial detection." Thesis, University of Reading, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.731708.

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Various aspects in the field of chromogens were studied. In a multifaceted approach, investigations into their synthesis, coupling to less common sugars, and screening as substrates for biological activity, together with kinetic studies on the rate of hydrolysis of indoxyl substrates were carried out. A three-step route to synthesise substituted indoxyl chromogens was successfully developed. This method was subsequently used to prepare a number of halogen derivatives to study the effect of halogen type and position of substitution on the reaction yields. Overall yields range between 2 and 27 %
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Sidibeh, Cherno Omar. "Production and cleavage specificity determination of serine proteases mMCP-4, mMCP-5, rMCP-2 and two platypus serine proteases of the chymase locus." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-197088.

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Serine proteases are a family of enzymes with a wide array of functions across both eukaryotes and prokaryotes. Here we have attempted to produce the serine proteases rat mast cell protease 2 and mouse mast cell protease 5 in a culture of HEK 293 cells; and mouse mast cell protease 4, platypus granzyme B-like protease and platypus hypothetical protease in a baculovirus expression system. Following production we wanted to analyse these serine proteases using a phage display assay and a battery of chromogenic substrates.
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Huang, Zheng. "Studies of novel chromogenic substrates and immunomagnetic separation techniques for microbiological characterization and detection." Thesis, King's College London (University of London), 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.415119.

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Gamage, Sujatha Nandani. "A study of catalytic autoxidation of organic substrates using H2/O2 mixtures in the presence of rhodium complexes containing dimethylsulfoxide ligands." Thesis, University of British Columbia, 1985. http://hdl.handle.net/2429/25791.

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Dimethylacetamide (DMA) solvent is oxidized catalytically to CH₃CON(CH₃)CH₂OOH and CH₃CON(CH₃)CHO under H₂/0₂ mixtures at 50°C in the presence of the dimethylsulfoxide complex RhCl₃(DMSO)₃ (I) at a rate which is much faster than peroxide-initiated autoxidation of DMA under O₂ alone. The hydroperoxide is thought to be the initial product, and the N-formyl derivative its decomposition product. An accompanying metal-catalyzed hydrogenolysis of 0₂ leads to H₂0₂ and H₂0. Hydrogen peroxide and CH₃CON(CH₃)CH₂OOH are the only products formed in the early stages of the catalytic reaction. The maximum r
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Bedernjak, Alexandre. "Synthesis and biological evaluation of novel chromogenic substrates for the enhanced detection of pathogenic bacteria." Thesis, University of Sunderland, 2010. http://sure.sunderland.ac.uk/6561/.

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The present work investigated the preparation of phenoxazinone derivatives and evaluated their performances for the detection of pathogenic bacteria. The first method investigated the condensation of nitroaminophenol with tetrahalogenobenzoquinones; the corresponding nitrohalogenophenoxazinones were all characterised and evaluated for the detection of nitroreductase activity in a range of clinically important microorganisms. The detection of nitroreductase activity has been previously suggested for the monitoring of bacterial growth; however, nitrohalogenophenoxazinones were proven to be less
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Abuaita, Areej, and Saleh Asmaa El. "Utvärdering av analysmetod för bestämning av anti-FXa aktivitet i plasma hos patienter behandlade med apixaban eller LMH." Thesis, Hälsohögskolan, Högskolan i Jönköping, HHJ, Avd. för naturvetenskap och biomedicin, 2019. http://urn.kb.se/resolve?urn=urn:nbn:se:hj:diva-45236.

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Apixaban och lågmolekylärt heparin (LMH) är antikoagulantia som förhindrar blodproppsbildning genom att hämma faktor Xa. Allt mer patienter använder apixaban och LMH, vilket gör att laboratoriemedicin på länssjukhuset Ryhov är i behov av att utvärdera analysmetoder för apixaban och LMH för att kunna implementera analyserna i klinisk rutin. Syftet med studien var att utvärdera analysmetoden för bestämning av anti-FXa aktivitet i plasma hos patienter behandlade med apixaban eller LMH med hjälp av kromogen substratmetod. Metodutvärderingen bestod av fyra steg: repeterbarhet, mel
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Chen, Jo-Chin, and 陳若瑾. "3D-Printed, Peroxidase Mimic/Chromogenic Substrate-Incorporated Multi-Well Device for in Situ Glucose Determination." Thesis, 2017. http://ndltd.ncl.edu.tw/handle/w3er3z.

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碩士<br>國立清華大學<br>生醫工程與環境科學系<br>105<br>Nanomaterials with intrinsic peroxidase-like activities have been demonstrated as promising artificial enzymes for numerous biochemical applications. In recent years, three dimensional printing (3DP) technologies have accelerated the customization and rapid prototyping of multilayer components/devices in general laboratories for a wide range of analytical applications. In this study, to enable the 3D-printed devices to have both the peroxidase and chromogenic activities, a multi-well plate is one-step printed using a dual-head fused deposition modeling-type
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Books on the topic "Chromogenic substrates"

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Lijnen, H. R. Synthetic Substrates in Clinical Blood Coagulation Assays. Springer, 2011.

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Witt, Irene, and Deutsche Gesellschaft für Klinische Chemie. New methods for the analysis of coagulation using chromogenic Substrates: Proceedings of the symposium of the Deutsche Gesellschaft für Klinische Chemie, Titisee, Breisgau, West-Germany, July 1976. De Gruyter, Inc., 2019.

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Book chapters on the topic "Chromogenic substrates"

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Kirschke, H., and B. Wiederanders. "Chromogenic Peptide Substrates." In Proteolytic Enzymes. Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_2.

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Porstmann, Bärbel, and Tomas Porstmann. "Chromogenic Substrates for Enzyme Immunoassay." In Nonisotopic Immunoassay. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5466-6_3.

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Zhang, Ruo-heng, Xue Ge, Xiao-jie Xu, and You-qi Tang. "Kinetic investigation of the chromogenic peptide substrates for chymotrypsin." In Peptides. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-010-9066-7_81.

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Biely, Peter. "Differentiation of Glycanases of Microbial Cellulolytic Systems Using Chromogenic and Fluorogenic Substrates." In Extracellular Enzymes of Microorganisms. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1274-1_23.

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Rijkers, D. T. S., H. C. Hemker, and G. I. Tesser. "Peptide p-nitroanilides: Chromogenic substrates for the determination of the thrombin generation curve." In Peptides 1994. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_415.

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Friberger, P. "Use of Chromogenic Peptide Substrates in the Study of Proteolytic Enzymes and Mechanisms Regulating them." In Cells, Membranes, and Disease, Including Renal. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1283-3_34.

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Schückel, Julia, and Stjepan Krešimir Kračun. "Two-Dimensional High-Throughput Endo-Enzyme Screening Assays Based on Chromogenic Polysaccharide Hydrogel and Complex Biomass Substrates." In Cellulases. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7877-9_15.

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Aasen, A. O. "Chromogenic Peptide Substrate Assays." In Update in Intensive Care and Emergency Medicine. Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-83042-6_16.

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Pennington, M. W., S. M. Festin, M. L. Maccecchini, F. Dick, and P. E. Scarborough. "HIV protease, chromogenic substrate and inhibitor." In Peptides 1990. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_326.

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Hahn-Hägerdal, Bärbel, and Anneli Svensson. "A Chromogenic Substrate Limulus Assay Applied to Raw Milk." In MILK the vital force. Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-3733-8_110.

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Conference papers on the topic "Chromogenic substrates"

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Stüber, W., D. Schiwek, U. Becker, and N. Heimburger. "NEW CHROMOGENIC SUBSTRATES FOR THE DETERMINATION OF COAGULATION AND FIBRINOLYSIS ENZYMES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644323.

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A new type of chromogenic substraces based on derivatives of phenoxazine is presented. Particularly interesting is the blue dye 7-amino-3-diethylamino-8-methylphenoxazine (ADMP) with a molar extinktion coefficient of about 80,000 at 624 nm. Peptides were linked to the aminogroup of the dye and red coloured substrates were obtained with a λmax value of about 540 nm. On account of the distinct difference of the λmax values and the negligable influence of the absorption peaks of the acylated and the free dye this chromophore is suitable for the synchesis of substrates. Besides the spectral proper
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Baumann, Martin J., Tuula T. Teeri, and Harry Brumer. "SYNTHESIS OF CHROMOGENIC AND FLUOROGENIC XYLOGLUCO-OLIGOSACCHARIDES AS SUBSTRATES FOR ENDOGLUCANASES AND XYLOGLUCAN ENDOTRANSGLYCOSYLASES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.730.

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Siekmann, U., D. Dittrih, and R. E. Zimmermann. "PHOTOMETER-LINKED MICROCOMPUTER SYSTEM ENABLES PRECISE CHROMOGENIC PROTHROMBIN TIME ASSAYS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644809.

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In coagulation diagnostics photometric assay procedures are in widespread use. Due to the availability of new specific chromogenic peptide substrates, automated instruments play an important role in clinical routine laboratory diagnosis. For research work, the benefit of expensive industrial photometric coagulation systems is questionable, especially as the program cannot be adapted by the user. For this purpose we developed an inexpensive microcomputer-controlled measuring system as well as a suitable photometric assay which allows to determine chromogenic clotting times with any conventional
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Fenton, J. W., J. I. Witting, and T. M. Miller. "THROMBIN KINETIC PARAMETERS WITH TRIPEPTIDE p-NITROANALIDES UNDER PHYSIOLOGICALLY RELEVANT CONDITIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643278.

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The Michaelis-Menten (Km ), catalytic (kcat ), and specificity (kcat/Km ) constants were determined for humSft α- and β-thrombins with the chromogenic substrate S-2238 (H-D-Phe-Pip-Arg-pNA), Chromozym-TH (Tos-Gly-Pro-Arg-pNA), and Spectrozyme-TH (H-D-HHT-Ala-Arg-pNA) in 0.15 M NaCl buffered with 10 mM HEPES ancTlO mM Tris-HCT at pH 7.4, 37°C. Spontaneous hydrolysis was insignificant for these substrates. Both S-2238 and Spectrozyme-TH exhibited limiting solubilities at ∼35 μM, while Chromozym-TH did not do so up to 50 μM. From initial estimates, Km's and k t's were refined by computer Gause-Ne
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Tans, G., T. Janssen-Claessen, J. Rosing, and J. H. Griffin. "APPLICATION OF SPECIFIC SERINE PROTEASE INHIBITORS IN ASSAYS FOR ACTIVATED CONTACT FACTORS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643301.

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We developed amidolytic assays to determine human Factor Xlla, Factor XIa and plasma kallikrein in mixtures containing variable amounts of each enzyme. The commercially available chromogenic substrates pro-phe-arg-pNA (S2302 or chromozym PK), glu-pro-arg-pNA (S2366), ile-glu-(piperidyl)-gly-arg-pNA (S2337), and ile-glu-gly-arg-pNA (S2222) were tested for their suitability as substrates in these assays. 8-Factor Xlla, Factor XIa and plasma kallikrein each exhibit considerable activity towards a number of these substrates. This precludes direct quantitation of the individual enzymes when large a
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Exner, T. "CONCENTRATION DEPENDENCE OF ACTIVATION OF ACARBOXYPROTEIN C BY THE CONTORTRIX ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644301.

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The protein C activator in Southern Copperhead (Agkistrodon Contortrix Contortrix) venom was isolated by sequential chromatographies on SP�Sephadex, Con A Sepharose and hydroxylapatite. It was found to be a single chain glycoprotein with an apparent molecular weight of 36,000 and an enzymatic specificity on chromogenic substrates resembling kallikein.This "contortrix activator" was used in a solid-phase immunochromometric assay (ICMA) for functional protein C in which heterologous antibody against protein C was passively coated onto microtitre wells and used to immoblize protein C. This was th
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Chmielewska, J., and B. Wiman. "ON THE KINETICS OF THE INHIBITION OF PLASMINOGEN ACTIVATORS BY THE PLASMINOGEN ACTIVATOR INHIBITOR PAI-1." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642808.

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The kinetics of the inhibition of the following plasminogen activators: one- and two-chain tissue plasminogen activator (t-PA) and low and high molecular weight urokinase (UK) by PAI-1 was studied. For this purpose direct systems were employed and the reactions were studied in the presence of different concentrations of plasminogen activator chromogenic substrates. The second-order rate constant of the association reaction was estimated from the initial decline in plasminogen activator activity. Determination of the rate constants in the absence of substrates was performed by plotting the rate
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Ellis, V., M. F. Scully, and V. V. Kakkar. "PLASMINOGEN ACTIVATION BY SINGLE-CHAIN UROKINASE (scu-PA) IN FUNCTIONAL ISOLATION - DEMONSTRATION OF A NOVEL MECHANISM." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642907.

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The kinetics of the activation of Glu- and Lys- plasminogen by single-chain urokinase (pro-urokinase) derived from the transformed human kidney cell line, TCL-598, has been studied and compared with two-chain urokinase (UK). Plasminogen activation was determined by the change in fluorescence polarization of fluorescein-labelled aprotinin (Trasylol), an essentially irreversible inhibitor of plasmin. This methodology allows plasmin production by scu-PA to be measured in functional isolation, with no interfering generation of two-chain UK. scu-PA was found to activate plasminogen to plasmin with
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Chabbat, J., L. Pejaudier, V. Kichenin-martin, S. Hampikian-Le Nin, and M. Steinbuch. "PROPERTIES OF A F VII CONCENTRATE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643282.

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A concentrate of factor VII obtained by adsorption onto an inorganic adsorbent using a by-product of routine fractionation as starting material This fraction contains only small amounts of the other constituents of the prothrombin complex ( PC ) but it is enriched in proteins C and S. It contains much less VIII CAg than the usual even activated PC concentrates. The amounts of isoagglutinins anti-A and B have also been checked. The concentrate of partially versus completely activated factor VII ( by factor Xlla ) has been submitted to animal experiences including those effected on hemophilic do
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Petersen, L. C., M. Johannessen, D. Foster, A. Kumar, and E. Mulvihill. "CATALYTIC ACTIVITIES OF ONE-CHAIN tPA AS REVEALED BY AN ANALOGUE RESISTANT TO PLASMIN CLEAVAGE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643845.

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Substitution of Arg275 with Gly in the activation site of tPA provides a one-chain recombinant analogue, tPA-Gly275, which is very resistant to cleavage by plasmin. The amidolytic activity of tPA-Gly275 with simple synthetic substrates was investigated and compared to the kinetics obtained with authentic one- and two-chain tPA. Both one-chain (zymogen) forms possess enzymatic activity, however, in the absence of fibrin it is much lower than that of two-chain tPA. Fibrin enhances the activity of the one-chain tPA forms, but not of two-chain tPA.A chromogenic assay was developed for measurement
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