Primary Structure of Human Fibrinogen
作者： Bengt GARDLUND , Birgit HESSEL , Birger BLOMBACK , Gerard MARGUERIE , Genesio MURANO
DOI: 10.1111/J.1432-1033.1977.TB11704.X
关键词: Protein primary structure 、 Alkylation 、 Molecule 、 Monomer 、 Chemistry 、 Chain (algebraic topology) 、 Fibrinogen 、 Polymer chemistry 、 Peptide 、 Stereochemistry 、 Peptide sequence
摘要: Five disulfide-containing fragments obtained from cyanogen-bromide-cleaved human fibrinogen (N-DSK, Hi2-DSK, Ho1-DSK, Ho2-DSK and Ho3-DSK) have been characterized in this report. The complete primary structure of the ‘N-terminal disulfide knot’, N-DSK, has elucidated earlier. individual chains composed more than one chain purified following reduction alkylation. Hi-2-DSK, Mr 26600, a one-chain fragment with intra-chain bond is derived Aα fibrinogen. 43000, consists five linked together by six bridges. largest 21000, γ fibrinogen, smaller chain, 5900, three remaining, 5800, 4300 2200, Bβ chain. Ho2-DSK, 5400, constitutes single-chain peptide bond. Ho3-DSK, 7400, two connected bridge. Amino acid analysis knots their presented. Partial amino sequence four larger Ho1-DSK smallest shown. All except N-DSK were found to be monomeric. One mole moles each other are present per These account for all disulfides (fraction 1–4). location molecule arrangement bonds discussed.
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