Biosynthesis of human cystathionine beta-synthase in cultured fibroblasts
作者： F Skovby , J P Kraus , L E Rosenberg
DOI: 10.1016/S0021-9258(17)43701-X
关键词: Cystathionine beta synthase 、 Proteolysis 、 Antiserum 、 Gel electrophoresis 、 Fibroblast 、 Biosynthesis 、 Protein subunit 、 Molecular biology 、 Biochemistry 、 Biology 、 ATP synthase
摘要: A single specific radiolabeled polypeptide with an apparent Mr = 63,000 was recovered when cystathionine beta-synthase (EC 4.2.1.22) precipitated from extracts of cultured human fibroblasts antiserum raised against pure liver synthase, and the immunocomplexes were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Partial proteolysis this fibroblast subunit synthase (Mr 48,000) produced similar peptide patterns. Pulse-chase experiments, however, did not provide any evidence for post-translational modification into a smaller "hepatic" form. Immunoprecipitation polypeptides synthesized in vitro mRNA revealed same mobility on electrophoresis as found whole cell extracts. We conclude that is primary translational product gene fibroblasts.
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