PARTIAL CHEMICAL CHARACTERIZATION OF ISOLATED GAMMA-CHAIN OF HUMAN FIBROGEN

被引:24
作者
MILLS, DA
LIENER, IE
机构
[1] Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
D O I
10.1016/0003-9861(69)90080-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The S-sulfo-γ-chain of human fibrinogen has been isolated and characterized with respect to end terminal groups, molecular weight, and amino acid and carbohydrate composition. The molecular weight, as determined by the isotopic recovery of the N-terminal amino acid, tyrosine, was 47,000-50,000. The C-terminal sequence revealed by the action of carboxypeptidase A was -(Ser, Ala, Gly)-Asp-Val. Two glycopeptides isolated from a tryptic digest of S-sulfo-γ-chain were found to contain essentially all of the solubilized carbohydrate. A single site of attachment of the carbohydrate moiety (3 glucosamine and 7 hexose residues) to the peptide chain is postulated. © 1969.
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页码:629 / &
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