Properties and specificity of a second metal chelator-sensitive proteinase in the keratinolytic larvae of the webbing clothes moth.
The properties of a second metal chelator-sensitive proteinase (metalloproteinase 2) from the larvae of the webbing clothes moth, Tineola bisselliella, have been studied. The pH optimum for casein digestion was 9-4 and the enzyme showed high stability between pH 8 and 11, but very poor stability at acid pH. The proteinase was inhibited by EDTA, but not by an EDTA-calcium complex. EDTA inhibition could be reversed by addition of a slight excess of calcium or zinc ions. The cleavage specificity of metalloproteinase 2 against the A and B chains of S-carboxymethyl insulin was almost identical to that found previously for metalloproteinase 1.
D000818:Animals; D004355:Drug Stability; D004492:Edetic Acid; D006863:Hydrogen-Ion Concentration; D007328:Insulin; D007814:Larva / Q000201:enzymology; D007915:Lepidoptera / Q000201:enzymology*; D009036:Moths / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification; D011480:Protease Inhibitors
D007328:Insulin; D011480:Protease Inhibitors; D004492:Edetic Acid; D010447:Peptide Hydrolases