Properties and specificity of a second metal chelator-sensitive proteinase in the keratinolytic larvae of the webbing clothes moth.
Aust J Biol Sci, 1975/12;28(5-6):439-45.
PMID: 5070
Abstract
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.
MeSH terms
Animals; Drug Stability; Edetic Acid; Hydrogen-Ion Concentration; Insulin; Larva; Lepidoptera; Moths; Peptide Hydrolases; Protease Inhibitors
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