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Inhibition of blood coagulation factors by serine esterase inhibitors
Author(s) -
De Lange J.A.,
Hemker H.C.
Publication year - 1972
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(72)80369-7
Subject(s) - citation , serine , medicine , chemistry , library science , biochemistry , enzyme , computer science
The reaction mechanism of blood coagulation presumably comprises a series of proenzyme-enzyme conversiqns, In a strict sense this has only been proven for prothrombin (factor II) which has been shown upon activation to yield the serine esterase thrombin I l ] . The coagulation factors II, VII, IX and X have much in common, both in the way of synthesis (dgpendence upon vitamio K) and physicochemical plgperties [2]. It therefole is conceivable that these fqur factors are proenzymes of serine esterases, that is they are serine esterases when in their activated forms*. It has been shown that factor Xu can split organic esters and is inhibited by DFP [3]. No enzymatic properties have been found to the fgptors Vu and VIII. [18, 19] . We qet out to investigate the inhibitory action of a sel of 25 known serine esterase inhibitors on the activities of coagulation factors II, V, VII, VIII, IX and X with the purpose of finding out which of these were serine esterases. We also hoped to finfl specific inhibitors for epch factor which would qreatly facilitate furtt-rg1 research in blood coazulation.