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Biosynthesis of human cystathionine beta-synthase in cultured fibroblasts.

Authors
  • Skovby, F
  • Kraus, J P
  • Rosenberg, L E
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Jan 10, 1984
Volume
259
Issue
1
Pages
583–587
Identifiers
PMID: 6706952
Source
Medline
License
Unknown

Abstract

A single specific radiolabeled polypeptide with an apparent Mr = 63,000 was recovered when cystathionine beta-synthase (EC 4.2.1.22) was precipitated from extracts of radiolabeled cultured human fibroblasts with an antiserum raised against pure human liver synthase, and the immunocomplexes were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Partial proteolysis of this fibroblast subunit and of the subunit of pure human liver synthase (Mr = 48,000) produced similar peptide patterns. Pulse-chase experiments, however, did not provide any evidence for post-translational modification of the fibroblast synthase subunit into a smaller "hepatic" form. Immunoprecipitation of polypeptides synthesized in vitro from human fibroblast mRNA revealed a polypeptide with the same mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as the synthase subunit found in whole cell extracts. We conclude that the Mr = 63,000 subunit is the primary translational product of the gene for cystathionine beta-synthase in human fibroblasts.

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