نتایج جستجو برای: thrombin like enzyme

تعداد نتایج: 890746  

Journal: :Annals of the rheumatic diseases 1994
R Morris P G Winyard D R Blake C J Morris

Accepted for publication 15 September 1993 Thrombin is classically recognised as factor IIa of the coagulation cascade, where it catalyses the conversion of fibrinogen into fibrin and so aids in the formation of a blood clot. Active thrombin is generated from prothrombin at the cell surface of platelets, lymphocytes, monocytes, neutrophils and endothelial cells.' It belongs to the serine protea...

Journal: :The Journal of biological chemistry 2009
Weiling Niu Zhiwei Chen Leslie A Bush-Pelc Alaji Bah Prafull S Gandhi Enrico Di Cera

The molecular mechanism of thrombin activation by Na(+) remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na(+) forms. The extended scheme establishes that analysis of k(cat) unequivocally identifies allosteric transduction of Na(+) binding into...

Journal: :The Journal of Experimental Medicine 1983
R A Wetsel W P Kolb

Experimental conditions required for the expression of maximum C5 activation upon limited trypsin hydrolysis were determined to be 0.008 mol of trypsin/mol C5 in a reaction mixture containing 1 mg C5/ml veronal-buffered saline incubated at 37 degrees C for 30 min. Employing these optimal incubation conditions, the primary or preferred site of trypsin hydrolysis of the C5 alpha-chain resulted in...

Journal: :The Journal of clinical investigation 1978
M Gramse C Bingenheimer W Schmidt R Egbring K Havemann

We investigated the effect of elastase-like neutral protease isolated from human granolocytes on human fibrinogen. Dependent on enzyme concentration and time of incubation, the elastase-like protease induced a progressive degradation of fibrinogen. Analysis of the remaining polypeptide chains showed a high susceptibility of the Aalpha- and low susceptibility of the gamma-chain of fibrinogen tow...

Journal: :Protein science : a publication of the Protein Society 2004
Elsa S Henriques Nelson Fonseca Maria João Ramos

Pit viper venoms contain a number of serine proteinases that exhibit one or more thrombin-like activities on fibrinogen and platelets, this being the case for the kinin-releasing and fibrinogen-clotting KN-BJ from the venom of Bothrops jararaca. A three-dimensional structural model of the KN-BJ2 serine proteinase was built by homology modeling using the snake venom plasminogen activator TSV-PA ...

Journal: :Biochemistry 2011
Weiling Niu Zhiwei Chen Prafull S Gandhi Austin D Vogt Nicola Pozzi Leslie A Pelc Fatima Zapata Enrico Di Cera

Protein allostery is based on the existence of multiple conformations in equilibrium linked to distinct functional properties. Although evidence of allosteric transitions is relatively easy to identify by functional studies, structural detection of a pre-existing equilibrium between alternative conformations remains challenging even for textbook examples of allosteric proteins. Kinetic studies ...

Journal: :The Journal of Experimental Medicine 1937
Harry Eagle

Nine of the 17 venoms here tested were found capable of coagulating citrated blood or plasma. As has been believed by most workers in the field, 7 of these 9 coagulant venoms convert fibrinogen to an insoluble modification resembling fibrin (Bothrops atrox, Bothrops jararaca, Bothrops nummifera, Crotalus adamanteus, Crotalus horridus, Crotalus terrificus basiliscus, Crotalus terrificus terrific...

Journal: :Computers in biology and medicine 1994
H Kessels G Willems H C Hemker

Thrombin is the central enzyme of haemostasis. Information on the production and inhibition of thrombin in plasma is important for evaluating the state of the coagulation system. Measurement of thrombin generation in plasma using small oligopeptide chromogenic substrates gives rise to a signal that not only reflects the enzymatic activity of free thrombin, but also contains a contribution of th...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1993
B E Maryanoff X Qiu K P Padmanabhan A Tulinsky H R Almond P Andrade-Gordon M N Greco J A Kauffman K C Nicolaou A Liu

The macrocyclic peptide cyclotheonamide A (CtA), isolated from the marine sponge Theonella sp., represents an unusual class of serine protease inhibitor. A complex of this inhibitor with human alpha-thrombin, a protease central to the bioregulation of thrombosis and hemostasis, was studied by x-ray crystallography. This work (2.3-A resolution) confirms the structure of CtA and reveals intimate ...

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