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• W2032032703 startingPage "371" @default.
• W2032032703 abstract "1. Four different fibrinopeptides, A, AP, Y and B, have been isolated from human fibrinogen by means of chromatography and precipitation procedures. 2. The amino acid sequence has been determined with the phenylisothiocyanate degradation method and by means of fragmentation with proteolytic enzymes and partial acid hydrolysis. The A-, AP- and Y-peptides are similar in structure, the AP-peptide being an A-peptide phosphorylated at the serine residue in Position 3 from the N-terminal end and the Y-peptide being one amino acid residue shorter than the A-peptide from the N-terminal end. The B-peptide has been found to have pyroglutamic acid as N-terminal residue. 3. The phosphorus in human fibrinogen is partly bound to an AP-peptide and partly to other structures of the fibrinogen molecule. 4. On basis of the results the structure of human fibrinogen and the specificity of thrombin is discussed." @default.
• W2032032703 created "2016-06-24" @default.
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• W2032032703 date "1966-02-01" @default.
• W2032032703 modified "2023-10-13" @default.
• W2032032703 title "Human fibrinopeptides isolation, characterization and structure" @default.
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• W2032032703 doi "https://doi.org/10.1016/0304-4165(66)90437-5" @default.
• W2032032703 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/5943441" @default.
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