Literature DB >> 656438

In vitro prothrombin synthesis from a purified precursor protein. II. Partial purification of bovine carboxylase.

C Vermeer, B A Soute, H C Hemker.   

Abstract

In this paper, we describe the isolation and partial purification of an enzyme system that converts bovine decarboxyfactor II (PIVKA-II) into prothrombin (factor II). It is shown that the increase in factor II activity occurs in parallel with 14CO2 incorporation into BaSO4 adsorbable proteins. The system is not strictly vitamin K-dependent because it is obtained from the livers of normal healthy cows. By preincubating the enzyme(s) with an excess of warfarin, an absolute vitamin K1-dependence can be obtained. The reaction is inhibited by its own product, factor II.

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Year:  1978        PMID: 656438     DOI: 10.1016/0005-2744(78)90052-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

Review 1.  Post-translational carboxylation of preprothrombin.

Authors:  B C Johnson
Journal:  Mol Cell Biochem       Date:  1981-08-11       Impact factor: 3.396

2.  Vitamin K-dependent carboxylase: evidence for a hydroperoxide intermediate in the reaction.

Authors:  A E Larson; J W Suttie
Journal:  Proc Natl Acad Sci U S A       Date:  1978-11       Impact factor: 11.205

Review 3.  The vitamin K-dependent carboxylation reaction.

Authors:  C Vermeer
Journal:  Mol Cell Biochem       Date:  1984       Impact factor: 3.396

4.  Characterization of vitamin K-dependent carboxylase from the livers from the adult ox and dicoumarol-treated calf.

Authors:  L Uotila; J W Suttie
Journal:  Biochem J       Date:  1982-02-01       Impact factor: 3.857

5.  Vitamin K-dependent carboxylation and vitamin K metabolism in liver. Effects of warfarin.

Authors:  R Wallin; L F Martin
Journal:  J Clin Invest       Date:  1985-11       Impact factor: 14.808

  5 in total

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