fibrinopeptide-a and aziridine

fibrinopeptide-a has been researched along with aziridine* in 1 studies

Other Studies

1 other study(ies) available for fibrinopeptide-a and aziridine

ArticleYear
Fibrinogen Bergamo I (A alpha 16Arg----Cys): susceptibility towards thrombin following aminoethylation, methylation or carboxamidomethylation of cysteine residues.
    Thrombosis and haemostasis, 1985, Aug-30, Volume: 54, Issue:2

    An abnormal fibrinogen, denoted as "fibrinogen Bergamo I", has been characterized. Its defect consists in an exchange of arginine by cysteine in position 16 of the A alpha-chain, thus corresponding to that found in a number of other fibrinogen variants. The abnormal fibrinopeptide A cannot be split off by thrombin from intact fibrinogen Bergamo I. We describe three different chemical modifications of the cysteine A alpha 16, i.e. aminoethylation, methylation and carboxamidomethylation, and their effects on the susceptibility of fibrinogen Bergamo I towards thrombin attack. S-aminoethylation of the A alpha 16Cys renders the peptide bond A alpha 16-17 cleavable by thrombin. Following methylation or carboxamidomethylation, the A alpha 19-arginyl bond becomes accessible for thrombin. The chemically modified extended fibrinopeptide A can be readily separated from the normal fibrinopeptide A by HPLC. The latter two modifications are suitable alternative procedures for detecting the molecular defect A alpha 16Arg----Cys of fibrinogen.

    Topics: Amino Acids; Aziridines; Blood Coagulation Disorders; Blood Coagulation Tests; Cysteine; Female; Fibrinogen; Fibrinogens, Abnormal; Fibrinopeptide A; Fibrinopeptide B; Humans; Male; Mercaptoethanol; Methylation; Thrombin

1985