Abstract
Comparative analysis of the influence of chlorine and fluorine anions on the fibrin polymerization
Highlights
Fibrinogen is one of the major proteins in the human hemostasis system
Two fibrinopeptides B are cleaved from the β-chains of the molecule and exposed the B polymerization sites, which increase the rate of polymerization, the branching of the fibrils and the formation of the fibrin clot network [6]
The influence of increasing concentrations of NaCl and NaF on the polymerization of fibrinogen activated by thrombin or ancistron
Summary
The reagents NaCl, NaF, Na2HPO4, NaH2PO4, NaOH, HCl, CaCl2, tris (three hydroxymethylaminomethan), HEPES (2-[4-(2-hydroxy) piperazine-1-il)ethanesulphonic acid, tween 20, water-soluble carbodiimide, N-hydroxysuccinimide, Gly-Pro-Arg-Pro peptide, heparin, thrombin, aprotinin were purchased from Sigma. The clot was formed in spectrophotometric cell, in which were consistently added a 0.02 M HEPES buffer, pH 7.4, containing NaCl or NaF at indicated concentration, and fibrinogen to a final concentration from 100 to 300 μg/ml. Exposure of neoantigenic determinant on fibri nogen molecule after cleavage of fibrinopeptides A under the action of thrombin or ancistron H was registered in real time using the plasmon resonance method and a plasmon spectropolarimeter device developed and manufactured at VE Lashkaryov Institute of Semiconductors of NAS of Ukraine, and an immunosensory chip with a covalently immobilized fibrin-specific monoclonal antibody FnI-3c. To investigate the effect of NaCl or NaF on the in situ interaction between fibrin and mAb FnI-3c, fibrinogen was passed into control cell at a concentration of 3-5 μg/ml in 0.02 M HEPES buffer, pH 7.4, a given salt concentration, 0.005% tween 20, and 1 mM concentration of GPRP peptide that blocked polymerization and supported fibrin molecules in monomeric form. The mean values of the parameters and their standard deviation were determined
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