[Effect of reduction of the interchain disulfide bridge of human thrombin on its enzymatic activity and structure].
It was shown that selective hydrolysis of the disulfide bridge between the A- and B-chains of human thrombin in the absence of denaturating agents decrease its proteolytic (e.g., fibrinogen-binding), esterase and amidase activities. Both chains remain bound by non-covalent interactions. A preparation of partially reduced thrombin was obtained and its kinetic parameters were determined. The experimental results suggest that the S-S bond connecting the A- and B-chains of thrombin is involved in the stabilization of the enzyme active center.
D002850:Chromatography, Gel; D004220:Disulfides / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence; D013438:Sulfhydryl Compounds / Q000032:analysis; D013917:Thrombin / Q000378:metabolism*
D004220:Disulfides; D013438:Sulfhydryl Compounds; D013917:Thrombin
Vliianie vosstanovleniia mezhtsepochechnogo disul'fidnogo mostika trombina cheloveka na ego fermentativnuiu aktivnost' i strukturu.