Structures of importance for the stability of antiplasmin as studied by site-directed mutagenesis.

doi:10.1016/j.thromres.2005.02.016

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Article

Structures of importance for the stability of antiplasmin as studied by site-directed mutagenesis.

Thrombosis research - 1 Jan 2006

Wang Haiyao, Pap Sarolta, Wiman Björn

Abstract excerpt

Human antiplasmin, a fast-acting inhibitor of plasmin in plasma, belongs to the serpin super-family of proteins. Like other members of this family, antiplasmin has a scissile peptide bond exposed within a reactive centre loop, typically present at the surface of the molecule. Antiplasmin is stable at neutral pH, but at acidic pH or at elevated temperatures it rapidly becomes inactivated. Data regarding "native"...

Topics

Animals
Antifibrinolytic Agents
Cell Line
DNA, Complementary
Drosophila
Electrophoresis, Polyacrylamide Gel
Genetic Variation
Humans
Hydrogen-Ion Concentration
Models, Molecular
Mutagenesis
Mutagenesis, Site-Directed
Mutation
Polymers
Protein Conformation
Protein Structure, Secondary
Reproducibility of Results
Serpins

Source

Open in PubMed

Identifiers

PMID: 16378834
DOI: 10.1016/j.thromres.2005.02.016

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