[Effect of reduction of the interchain disulfide bridge of human thrombin on its enzymatic activity and structure]

Autor: A A, Sereĭskaia, T V, Osadchuk, A I, Korneliuk, S B, Serebrianyĭ, S A, Atepalikhina
Rok vydání: 1986
Předmět:
Zdroj: Biokhimiia (Moscow, Russia). 51(10)
ISSN: 0320-9725
Popis: 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.
Databáze: OpenAIRE