[Enzymatic properties of the isolated B-chain of human thrombin].
The A- and B-chains have been isolated from the non-covalent complex of human thrombin A- and B-chains, using selective reduction of the interchain disulfide bridge. The B-chain thus isolated (de-A-thrombin) retains its conformation, which is close to the native one and thus differs considerably from the B-chain isolated from the fully reduced enzyme. Nevertheless, the proteolytic (in terms of fibrinogen clotting) and amidase activities of de-A-thrombin are markedly reduced as compared to the native enzyme and the non-covalent complex of A- and B-chains. It is assumed that the A-chain of thrombin is necessary for normal functioning of the active site of thrombin localized in the B-chain.
Sereĭskaia
A A
AA
Osadchuk
T V
TV
Korneliuk
A I
AI
Pekhnik
I V
IV
Serebrianyĭ
S B
SB
D004220:Disulfides / Q000378:metabolism; D006801:Humans; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012697:Serine Endopeptidases; D013917:Thrombin / Q000378:metabolism*
D004220:Disulfides; D012697:Serine Endopeptidases; D013917:Thrombin
Fermentativnye svoĭstva izolirovannoĭ B-tsepi trombina cheloveka.