Partial characterization of the extracellular keratinase from Microsporum canis.
The extracellular keratinase of Microsporum canis released peptides from alpha-type fibrous protein and the membranous fraction isolated from human stratum corneum. Inhibition of the enzyme by phenylmethyl-sulfonylfluoride and its weak inhibition by N-ethylmaleimide and etheneglycol tetra-acetic acid indicated that it is probably a serine proteinase.
D004533:Egtazic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004817:Epidermis; D005033:Ethylmaleimide / Q000494:pharmacology; D006801:Humans; D008864:Microsporum / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D011480:Protease Inhibitors
D011480:Protease Inhibitors; D004533:Egtazic Acid; D010664:Phenylmethylsulfonyl Fluoride; D010447:Peptide Hydrolases; C035855:keratinase; D005033:Ethylmaleimide