Article
Antithrombin Vicenza, Ala 384 to Pro (GCA to CCA) mutation, transforming the inhibitor into a substrate.
British journal of haematology - 1 Jan 1991
Caso R, Lane D A, Thompson E A, Olds R J, Thein S L, Panico M, Blench I, Morris H R, Freyssinet J M, Aiach M
Abstract excerpt
Antithrombin (AT) Vicenza has been previously identified as a functionally abnormal antithrombin associated with familial thrombosis (Finazzi et al, 1985). It binds normally to heparin, but loses its affinity following interaction with thrombin: it is a poor inhibitor of thrombin. AT Vicenza was isolated from plasma by heparin-Sepharose and thrombin-Sepharose chromatography, fragmented with cyanogen bromide...
Topics
- Amino Acid Sequence
- Antithrombin III
- Base Sequence
- Codon
- Electrophoresis, Polyacrylamide Gel
- Exons
- Humans
- Molecular Sequence Data
- Mutation
- Polymerase Chain Reaction
- Substrate Specificity