Affiliation:
1. Department of Microbiology, The University of British Columbia, Vancouver, British Columbia, Canada
Abstract
Inorganic phosphate was found to decrease the caseinolytic and ethyl-esterase activities of the
Microsporum gypseum
germination protease. The germination protease possessed exokeratinase (beta-keratinase) activity immediately after release from the fungal spore. After phosphate treatment of the enzyme, the germination protease also possessed endo-keratinase (alpha-keratinase) activity. Phosphate altered the protease's pH optimum from 9.0 to 7.0 and decreased the molecular weight from 33,000 to 16,000. These values were identical to those found for the keratinase. Alpha- and beta-keratinase activities were stimulated in excess of 200-fold by disulfide reducing agents. Natural and suspected keratin degradation products also enhanced keratinase activity. Cell fractionation and in vitro conversion of the alkaline germination protease into a functional keratinase suggested that the subunits comprising the germination protease and the keratinase were of a common origin.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference30 articles.
1. Alexander P. and R. F. Hudson. 1954. Wool its chemis-try and physics p. 340-350. Chapman Hall Ltd. London.
2. Boyer P. D. 1959. Sulfhydryl and disulfide groups of enzymes p. 511-588. In P. D. Boyer H. Hardy and K. Myrback (ed.) The enzymes vol. 1 2nd ed. Academic Press Inc. New York.
3. The effect of urea on hydrophobic bonds: the critical micelle concentration of n-dodecyltrimethylammonium bromide in aqueous solutions of urea;Bruning W.;J. Amer. Chem. Soc.,1961
4. The decomposition of wool keratin by Keratinomyces ajelloi;Chesters C. G. C.;Sabouraudia,1963
5. Dithiothreitol, a new protective reagent for SH groups;Cleland W. W.;Biochemistry,1964
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