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Peptidase activities in Group N streptococci

Published online by Cambridge University Press:  01 June 2009

Lynette Mou ,
J. J. Sullivan  and
G. R. Jago
Lynette Mou
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia
J. J. Sullivan
Affiliation:
Dairy Research Laboratory, Division of Food Research, C.S.I.R.O., Highett, Victoria 3190, Australia
G. R. Jago
Affiliation:
Dairy Research Laboratory, Division of Food Research, C.S.I.R.O., Highett, Victoria 3190, Australia
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Summary

Several peptidase activities in the 3 species of Group N streptococci were partly separated by gel filtration on Sephadex G-200. The peptidases identified were a general aminopeptidase of wide specificity, a tripeptidase, a proline iminopeptidase (prolyl-β-naphthylamidase), a proline iminodipeptidase and an aminopeptidase-P. The effects of temperature and pH on the stability of the enzyme activities, and the influence of the type of N source used in the growth medium on the elution pattern of the enzymes were examined.

Type
Research Article
Information
Journal of Dairy Research , Volume 42 , Issue 1 , February 1975 , pp. 147 - 155
Copyright
Copyright © Proprietors of Journal of Dairy Research 1975

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