Novel Structure Elucidation Strategy for Genetically Abnormal Fibrinogens with Incomplete Fibrinopeptide Release as Applied to Fibrinogen Schwarzach

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Abstract
A novel and simple strategy was developed for the structure elucidation of those genetically abnormal [human] fibrinogens in which thrombin is unable to release fibrinopeptide A from the abnormal molecules. The method provides evidence for the Arg .fwdarw. Cys exchange at the C-terminus of the fibrinopeptide A sequence. The abnormal fibrinogen was mercaptolysed and then S-aminoethylated. On thrombin digestion, the modified fibrinogen released new peptides, as shown by high-performance liquid chromatography. The amino-acid analysis proved that these peptides correspond to the expected fibrinopeptide A variants. The analyzed case of dysfibrinogenemia, designated Fibrinogen Schwarzach, contains an A.alpha. 16 Arg .fwdarw. Cys exchange in the heterozygous form.

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