Proteinase A (EC 22.214.171.124) was purified from commercial bakers' yeast in five steps, including hydrophobic chromatography and affinity chromatography. After the last step the enzyme appeared homogeneous on polyacrylamide gel electrophoresis and in the analytical ultracentrifuge. A molecular weight of 41,500 was determined for proteinase A. The amino acid composition includes 43% polar residues and 12% aromatic amino acids. Proteinase A is a glycoprotein containing 7.5% mannose and 1% of glucosamine and galactosamine. The temperature and the pH stability of the enzyme have been determined. At pH 6, the proteinase exhibits a remarkable stability even in 6 M urea. Proteinase A splits hemoglobin with an optimum at pH 3.0 and casein and azocasein with an optimum at pH 6.0. The enzyme is inhibited by pepstatin, diazoacetyl-DL-norleucine methyl ester and by 1,2-epoxy-3-(4-nitro-phenoxy) propane.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Annotation Extension||Reference|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Assay||Construct||Conditions||Strain Background||Reference|