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- W1646397714 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." @default.
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- W1646397714 date "1984-01-01" @default.
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- W1646397714 title "Biosynthesis of human cystathionine beta-synthase in cultured fibroblasts." @default.
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- W1646397714 doi "https://doi.org/10.1016/s0021-9258(17)43701-x" @default.
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