Abstract
The role of the 13 histidine residues in plasminogen activator inhibitor 1 (PAI-1) for the stability of the molecule was studied by replacing these residues by threonine, using site-directed mutagenesis. The generated mutants were expressed in Escherichia coli, purified and characterized. All variants had a normal activity and formed stable complexes with tissue-type plasminogen activator. Most of these PAI-1 variants displayed a similar pH-dependency in stability as wild-type PAI-1, with increased half-lives at lower pH. However, the variant His364Thr had a half-life of about 50 min at 37°C and had almost completely lost its pH-dependency. Therefore, our data suggest that His 364, in the COOH-terminal end of the molecule might be responsible for the pH-dependent stability of PAI-1.
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