Vitamin K-dependent carboxylase: the carboxylation of exogenous substrates in different systems

Marian A G de Boer-van den Berg, Magda M W Ulrich, H. Coenraad Hemker, Berry A M Soute, Cees Vermeer

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Two types of solid-phase carboxylase, SPC-II and SPC-X, have been prepared from the livers of warfarin-treated cows. Their enzymatic activities were compared with substrate-free carboxylase in microsomes from normal cows and substrate-bound carboxylase in microsomes from warfarin-treated cows. A number of exogenous substrates for carboxylase have been purified and tested. We found that large substrates, such as descarboxyprothrombin, are carboxylated only by substrate-free carboxylase and not by the substrate-bound enzyme. No differences in apparent Km values between solid-phase carboxylases II and X were observed.

Original languageEnglish
Pages (from-to)94-98
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume831
Issue number1
DOIs
Publication statusPublished - 20 Sep 1985

Cite this

de Boer-van den Berg, Marian A G ; Ulrich, Magda M W ; Hemker, H. Coenraad ; Soute, Berry A M ; Vermeer, Cees. / Vitamin K-dependent carboxylase : the carboxylation of exogenous substrates in different systems. In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1985 ; Vol. 831, No. 1. pp. 94-98.
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abstract = "Two types of solid-phase carboxylase, SPC-II and SPC-X, have been prepared from the livers of warfarin-treated cows. Their enzymatic activities were compared with substrate-free carboxylase in microsomes from normal cows and substrate-bound carboxylase in microsomes from warfarin-treated cows. A number of exogenous substrates for carboxylase have been purified and tested. We found that large substrates, such as descarboxyprothrombin, are carboxylated only by substrate-free carboxylase and not by the substrate-bound enzyme. No differences in apparent Km values between solid-phase carboxylases II and X were observed.",
keywords = "(Bovine liver), Carboxylase, Descarboxyfactor, Vitamin K, Warfarin",
author = "{de Boer-van den Berg}, {Marian A G} and Ulrich, {Magda M W} and Hemker, {H. Coenraad} and Soute, {Berry A M} and Cees Vermeer",
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Vitamin K-dependent carboxylase : the carboxylation of exogenous substrates in different systems. / de Boer-van den Berg, Marian A G; Ulrich, Magda M W; Hemker, H. Coenraad; Soute, Berry A M; Vermeer, Cees.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 831, No. 1, 20.09.1985, p. 94-98.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Vitamin K-dependent carboxylase

T2 - the carboxylation of exogenous substrates in different systems

AU - de Boer-van den Berg, Marian A G

AU - Ulrich, Magda M W

AU - Hemker, H. Coenraad

AU - Soute, Berry A M

AU - Vermeer, Cees

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AB - Two types of solid-phase carboxylase, SPC-II and SPC-X, have been prepared from the livers of warfarin-treated cows. Their enzymatic activities were compared with substrate-free carboxylase in microsomes from normal cows and substrate-bound carboxylase in microsomes from warfarin-treated cows. A number of exogenous substrates for carboxylase have been purified and tested. We found that large substrates, such as descarboxyprothrombin, are carboxylated only by substrate-free carboxylase and not by the substrate-bound enzyme. No differences in apparent Km values between solid-phase carboxylases II and X were observed.

KW - (Bovine liver)

KW - Carboxylase

KW - Descarboxyfactor

KW - Vitamin K

KW - Warfarin

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