Sulfation of a gamma-chain variant of human fibrinogen.
Biosynthetic sulfation of human fibrinogen was investigated using a hepatoma-derived cell line in culture. Very little [35]sulfate was incorporated into the major forms of the A alpha, B beta, or gamma-chains of fibrinogen, but there was a labeled peptide chain with electrophoretic mobility intermediate between the B beta and gamma-chains. Base hydrolysis of the sulfate-labeled product released tyrosine sulfate. The labeled peptide is identified as a form of gamma-chain by its resistance to proteolysis during extended periods of incubation, in contrast with A alpha and B beta-chains which are converted to smaller forms. The results indicate that human fibrinogen contains tyrosine sulfate primarily within a variant form of the gamma-chain.
Hortin
G L
GL
Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110.
D000595:Amino Acid Sequence; D006528:Carcinoma, Hepatocellular; D002852:Chromatography, Ion Exchange; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D008113:Liver Neoplasms; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D012689:Sequence Homology, Nucleic Acid; D013431:Sulfates / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D013431:Sulfates; C005662:tyrosine O-sulfate; D014443:Tyrosine; D005340:Fibrinogen