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- W2024558695 abstract "The investigation aimed at preparing peptide chains of human fibrin and fibrinogen suitable, in quantity and chemical form, for determination of the primary structure. 10 g of fibrin or fibrinogen were mercaptolysed with mercaptoethanol, and subsequently carboxymethylated with iodoacetate, all in 9 M urea. The conditions used led to complete and selective conversion of cystine residues to S-carboxymethylcysteine residues. 5–10 g of S-carboxymethylfibrin were fractionated by chromatography on CM-cellulose in 8 M urea with a pH gradient 4.80 to 6.00. Three major and two minor components were isolated. N-terminal sequence determination allowed the identification of the major components as the α-, β- and γ-chain, and the calculation of the molecular weights 75 000, 68 000 and 52 000, respectively. Amino acid composition and electrophoretic mobility are given for each chain. The minor components, by their N-terminal sequence, were clearly related to the γ-chain, but differed in amino acid composition, and were therefore designated γx and γy. They constituted 1% and 6%, respectively, of total γ-chain. The fibrinogen derivative was fractionated in a similar way, and also produced five components. The three major components were identified as the α(A)-, β(B)- and γ-chain by sequence determination and thrombin digestion. Unexpectedly, thrombin released from the α(A)-chain not only fibrinopeptide A, but also a tripeptide, Gly-Pro-Arg. This could be placed in the sequence as following directly on the fibrinopeptide moiety. The minor components were tentatively identified with the γx- and γy-chains found in fibrin." @default.
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- W2024558695 title "Large scale preparation of S-carboxymethylated chains of human fibrin and fibrinogen and the occurrence of γ-chain variants" @default.
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- W2024558695 doi "https://doi.org/10.1016/0005-2795(72)90088-8" @default.
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