Literature DB >> 4040397

Isoenzymes of vitamin-K-dependent carboxylase.

M M Ulrich, B A Soute, M A de Boer-van den Berg, C Vermeer.   

Abstract

Vitamin-K-dependent carboxylase was prepared from bovine liver, kidney, lung and testis and it was checked that these systems obeyed the laws of normal enzyme kinetics. Four carboxylatable substrates were obtained from different sources and the apparent Michaelis constants of the various carboxylases for these four substrates were measured. From the results thus obtained we concluded that carboxylase is a group name for a number of isoenzymes which are present in hepatic as well as in various non-hepatic tissues.

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Year:  1985        PMID: 4040397     DOI: 10.1016/0167-4838(85)90138-4

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


  6 in total

1.  Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins.

Authors:  R J Houben; D Jin; D W Stafford; P Proost; R H Ebberink; C Vermeer; B A Soute
Journal:  Biochem J       Date:  1999-07-15       Impact factor: 3.857

2.  Characteristics and composition of the vitamin K-dependent gamma-glutamyl carboxylase-binding domain on osteocalcin.

Authors:  Roger J T J Houben; Dirk T S Rijkers; Thomas B Stanley; Francine Acher; Robert Azerad; Sanna-Maria Käkönen; Cees Vermeer; Berry A M Soute
Journal:  Biochem J       Date:  2002-05-15       Impact factor: 3.857

3.  Molecular cloning of matrix Gla protein: implications for substrate recognition by the vitamin K-dependent gamma-carboxylase.

Authors:  P A Price; J D Fraser; G Metz-Virca
Journal:  Proc Natl Acad Sci U S A       Date:  1987-12       Impact factor: 11.205

4.  The propeptide region of clotting factor IX is a signal for a vitamin K dependent carboxylase: evidence from protein engineering of amino acid -4.

Authors:  P Galeffi; G G Brownlee
Journal:  Nucleic Acids Res       Date:  1987-11-25       Impact factor: 16.971

5.  Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase.

Authors:  B A Soute; M M Groenen-van Dooren; A Holmgren; J Lundström; C Vermeer
Journal:  Biochem J       Date:  1992-01-01       Impact factor: 3.857

6.  Isolation and partial characterization of a vitamin K-dependent carboxylase from bovine aortae.

Authors:  L J Van Haarlem; M M Ulrich; H C Hemker; B A Soute; C Vermeer
Journal:  Biochem J       Date:  1987-07-01       Impact factor: 3.857

  6 in total

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