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  • Title: Fibrinogens Bern IV, Bern V and Milano XI: three dysfunctional variants with amino acid substitutions in the thrombin cleavage site of the Aalpha-chain.
    Author: Stucki B, Zenhäusern R, Biedermann B, Baudo F, Redaelli R, Lämmle B, Furlan M.
    Journal: Blood Coagul Fibrinolysis; 1999 Mar; 10(2):93-9. PubMed ID: 10192658.
    Abstract:
    Thrombin-induced cleavage of fibrinopeptide A is the initial step in the conversion of fibrinogen to fibrin. Three dysfunctional fibrinogen variants are described with an amino acid substitution at position 16 of the Aalpha-chain: the fibrinogen variants Bern IV and Milano XI having an Arg-->His substitution and the variant Bern V having an Arg-->Cys substitution. Routine coagulation studies revealed prolonged plasma thrombin and reptilase clotting times in all patients, and a discrepancy between the plasma levels of fibrinogen determined by the clotting assay and electroimmunoassay. The defect was localized by high-performance liquid chromatography analysis of fibrinopeptide release and confirmed by polymerase chain reaction and sequencing of exon 2 of the Aalpha-chain. Immunoblotting analysis with a rabbit antiserum against human serum albumin indicated that albumin was linked to the additional sulfhydryl group of fibrinogen Bern V. The assay of tissue-plasminogen-activator-induced plasmic degradation revealed that the fibrinolysis of fibrin Bern V was delayed, whereas fibrin Bern IV was digested in the same way as normal fibrin.
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