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Partial purification of bovine liver vitamin K‐dependent carboxylase by immunospecific adsorption onto antifactor X
Author(s) -
De Metz M.,
Vermeer C.,
Soute B.A.M.,
Van Scharrenburg G.J.M.,
Slotboom A.J.,
Hemker H.C.
Publication year - 1981
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(81)80290-6
Subject(s) - chemistry
Administration of vitamin K-antagonists induces the appearance of abnormal clotting factors in the blood (man, cow) or in the liver (rat). These abnormal clotting factors (descarboxyfactors) contain glutamic acid (Glu) residues instead of the y-carboxyglutamic acid (Gla) residues, which occur in normal clotting factors [ 11. In human and bovine plasma -90% of the abnormal proteins consists of descarboxyprothrombin. Attempts to identify the rat liver abnormal proteins have been done in an in vitro vitamin K-dependent carboxylating enzyme system (carboxylase) and it was shown that only 25% of the carboxylated endogenous substrates bound to antiprothrombin antibodies [2]. Here, we describe the preparation of vitamin K-dependent carboxylase from the livers of warfarintreated cows and the results of our investigations concerning the distribution of the various clotting factor precursors in this enzyme system.