Thrombin enzyme
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A database containing chemical structures of 60 inhibitors and their Ki values was put into molecular operating environment (MOE) 2008.10 software, and the two-dimensional (2D) physicochemical descriptors were numerically calculated. After removing the irrelevant descriptors, a QSAR modeling was developed from the 2D-descriptors and Ki values by using the partial least squares (PLS) regression method.
5p larachdumlanat127 02-01-2021 20 2 Download
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A high-affinity monoclonal antibody (M27), raised against the human thrombin–antithrombin complex, has been identifiedand characterized. The epitope recognizedbyM27 was located to the linear sequence FIREVP (residues 411– 416), located in the C-terminal cleavage peptide of anti-thrombin.This regionoverlaps, by two residues, theputative binding site of antithrombin for the serpin–enzyme complex receptor.
11p tumor12 20-04-2013 37 4 Download
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Members of the serine protease inhibitor (serpin) superfamily play import-ant roles in the inhibition of serine proteases involved in complex systems. This is evident in the regulation of coagulation serine proteases, especially the central enzyme in this system, thrombin. This review focuses on three serpins which are known to be key players in the regulation of thrombin: antithrombin and heparin cofactor II, which inhibit thrombin in its pro-coagulant role, and protein C inhibitor, which primarily inhibits the throm-bin⁄thrombomodulin complex, where thrombin plays an anticoagulant role. .
10p fptmusic 12-04-2013 39 3 Download
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The effects of high hydrostatic pressure (HHP) and urea on conformational transitions of humana-thrombin structure were studiedbyfluorescence spectroscopy andbymeasuring the catalytic activity of the enzyme. Treatment of thrombin with urea produced a progressive red shift in the center of mass of the intrinsic fluorescence emission spectrum, with a maximum displacement of 650 cm )1 . HHP (270 MPa) shifted the centre ofmass by only 370 cm )1 .HHP combined with a subdenaturing urea concentration (1.5M) displaced the centre of mass by 750 cm )1 ....
8p dell39 03-04-2013 27 3 Download
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Procarboxypeptidase U [proCPU, thrombin-activatable fibrinolysis inhib-itor (TAFI), EC 3.4.17.20] belongs to the metallocarboxypeptidase family and is a zymogen found in human plasma. ProCPU has been proposed to be a molecular link between coagulation and fibrinolysis. Upon activation of proCPU, the active enzyme (CPU) rapidly becomes inactive due to its intrinsic instability.
15p dell39 27-03-2013 49 3 Download
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The catalytic competence of the natural thrombin mutant with deletion of the Lys9 residue in the A-chain (DK9) was found to be severely impaired, most likely due to modification of the 60-loop conformation and catalytic triad geometry, as supported by long molecular dynamics (MD) simula-tions in explicit water solvent.
11p dell39 27-03-2013 37 4 Download
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Vai trò chủ yếu của vitamin B6: A. Tham gia vào cơ chế nhìn của mắt B. Chống bệnh pellagra C. Tham gia vào quá trình đông máu D. Là coenzym của những enzym xúc tác cho phản ứng trao đổi amin và decarboxyl củamột số acid amin E. Chống bệnh tê phù. 2. Vitamin tham gia cấu tạo coenzymA là : A.Vitamin E B. Vitamin B5 C. VitaminA D.VitaminB E. VitaminK 3. Vitamin D cần thiết cho: A. Quá trình chuyển hóa Ca2+và phospho C. Chuyển prothrombin thành thrombin E. Chống thiếu máu. 4. Trong lipid có thể chưá...
9p buddy7 29-06-2011 552 50 Download
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Sites of action of the four major physiologic antithrombotic pathways: antithrombin (AT); protein C/S (PC/PS); tissue factor pathway inhibitor (TFPI); and the fibrinolytic system, consisting of plasminogen, plasminogen activator (PA), and plasmin. PT, prothrombin; Th, thrombin; FDP, fibrin(ogen) degradation products. [Modified from BA Konkle, AI Schafer, in DP Zipes et al (eds): Braunwald's Heart Disease, 7th ed. Philadelphia, Saunders, 2005.] Antithrombin (or antithrombin III) is the major plasma protease inhibitor of thrombin and the other clotting factors in coagulation.
5p konheokonmummim 03-12-2010 82 5 Download