Biosynthesis of Dog Fibrinogen

作者: Bohdan KUDRYK , Masahisa OKADA , Colvin M. REDMAN , Birger BLOMBÄCK

DOI: 10.1111/J.1432-1033.1982.TB06735.X

关键词:

摘要: Dogs were injected with 3H-labeled L-amino acids and the incorporation of radioactivity into fibrinogen, its component polypeptide chains various well characterized fibrinogen fragments, was determined in newly secreted plasma nascent isolated from rough endoplasmic reticulum hepatocytes. At 15-20 min after administration l-amino acids, radioactive onto blood specific radioactivities Aα, Bβ y approximately same at all times secretion up to 2 h. Newly almost entirely phosphorylated form. 15-18 min, a time which maximal had occurred proteins, deoxycholate-soluble fraction by affinity chromatography using columns fibrin monomer as those prepared monospecific antibodies dog chains. The thus further analyses thrombin- released fibrinopeptides A B their tryptic peptides. Furthermore, cleaved cyanogen bromide, NH2-terminal disulfide knot chain fragments peptides derived these isolated. it is concluded that three are synthesized extent that, within reticulum, has already been fully disulfide-bonded exists dimer. In contrast Aa not sulfated.

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