Action of clotting (α) and nonclotting (γ) thrombins on bovine fibrinogen N-terminal fragments

Sereyskaya, A. A.; Smirnova, I. V.

doi:10.7124/bc.0002D5

Biopolym. Cell. 1991; 7(3):82-89.

http://dx.doi.org/10.7124/bc.0002D5

Structure and Function of Biopolymers

Action of clotting (α) and nonclotting (γ) thrombins on bovine fibrinogen N-terminal fragments

1Sereyskaya A. A., 1Smirnova I. V.

Institute of Bioorganic Chemistry and Petrochemistry, Academy of Sciences of the Ukrainian SSR
Kiev, USSR

Abstract

Bovine fibrinogen N-terminal fragments were hydrolysed by native α-thrombin and its nonclotting γ-form (with disruptured additional centre for high molecular substrates recognition). It was found that susceptible bond 19–20 of Ace chain is cleaved by α-thrombin more efficiently than γ-form both in the structure of N-terminal disulfide knot and in the isolated Atx fragment 1–54. This difference disappears as a result of peptide bonds splitting due to Ace Trp36 and Trp44 modification. The rate of α-thrombin hydrolysis of modified substrates is lowered significantly ad reached the γ-thrombin level. The data presented here establish that 1) the specific site complementary to thrombin additional recognition centre is localized wiihinn the sequence 37–54 of bovine fibrinogen Act chain; 2) interactions between fibrinogen and thrombin recognition sites arc necessary for effective 19–20 bond hydrolysis.

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