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- W2147679875 abstract "Dysfunctional fibrinogen variants have been discovered by prolongation of thrombin and reptilase clotting times and a discrepancy of the functionally and immunologically determined fibrinogen concentration. More than 250 variants have been described (1). Majority of the abnormal fibrinogen variants have a structural defect near or at the thrombin cleavage site in the Aα-chain (2,3). Removal of fibrinopeptide A is required to expose the amino-terminal polymerization site (4,5). Most molecular defects in abnormal fibrinogen variants with normal fibrinopeptide A release but impaired fibrin monomer polymerization have been localized within residues γ 275 to γ 375 (1) containing the putative carboxy terminal polymerization site γ 337–379 (6,7). In the present report we describe another congenitally abnormal fibrinogen that was found in a 42-year-old asymptomatic woman and her son. A single amino acid substitution γ 275 Arg → His was found in this dysfunctional fibrinogen variant." @default.
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- W2147679875 date "1996-01-01" @default.
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- W2147679875 title "Fibrinogen Claro — Another dysfunctional fibrinogen variant with γ 275 Arginine → Histidine substitution" @default.
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- W2147679875 doi "https://doi.org/10.1016/0049-3848(95)00222-7" @default.
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