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Amino acid sequence of the beta chain of human fibrinogen.
The beta chain of human fibrinogen contains 461 amino acid residues, 15 of which are methionines. The calculated molecular weight, independent of a single carbohydrate cluster, is 52 230. In this regard, we have isolated and characterized all 16 cyanogen bromide fragments. In one case (CNI), we have concentrated on a disputed portion of a previously reported fragment. The arrangement of the cyanogen bromide peptides was deduced by the use of overlap fragments obtained from the tryptic digestion of modified and unmodified beta-chains and from digestions with staphylococcal protease, as well as by considerations involving the plasmic digestion products of fibrinogen. In one case two adjacent fragments were aligned by homology with the corresponding segments of the gamma chain. The homology of the beta chain with the gamma chain is especially strong over the course of the carboxy-terminal two-thirds of the sequence. Neither of these chains appears to be homologous with the alpha chain in these regions. With a few minor exceptions, the sequence reported in this article is in agreement with data reported by other groups in Stockholm and Munich.
PMID: 420779 [PubMed - indexed for MEDLINE]
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Cited by 7 PubMed Central articles
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Use of porcine fibrinogen as a model glycoprotein to study the binding specificity of the three variants of K88 lectin.
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[Infect Immun. 1995]
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Shadow-cast electron microscopy of fibrinogen with antibody fragments bound to specific regions.
Price TM, Strong DD, Rudee ML, Doolittle RF.
Proc Natl Acad Sci U S A. 1981 Jan; 78(1):200-4.
[Proc Natl Acad Sci U S A. 1981]
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Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen.
Imam AM, Eaton MA, Williamson R, Humphries S.
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[Nucleic Acids Res. 1983]
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