Some biochemical characteristics of a partially purified extracellular keratinase from Trichophyton schoenleinii.
A Trichophyton schoenleinii (T. schoenleinii) strain from tinea favus was cultured in a liquid medium, from which an extracellular keratinase extract was obtained. The keratinase was partially purified with carboxymethyl-cellulose (CMC) column chromatography. Some biochemical characteristics of the keratinase were then examined. Its molecular weight was estimated to be 38,000 on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal temperature was 50 degrees C, and the optimal pH value was 5.5. The keratinolytic activity was specifically increased by Fe++ and Fe .
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Department of Dermatology, Shimane Medical University, Izumo, Japan.
Dekio
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Jidoi
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D000818:Animals; D006168:Guinea Pigs; D006197:Hair / Q000378:metabolism / Q000382:microbiology*; D006801:Humans; D007633:Keratins / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D014249:Trichophyton / Q000201:enzymology*
D007633:Keratins; D010447:Peptide Hydrolases; C035855:keratinase