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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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References

REFERENCES

Davis, N. C. & Smith, E. L. (1953). Journal of Biological Chemistry 200, 373.CrossRefGoogle Scholar
Davis, N. C. & Smith, E. L. (1957). Journal of Biological Chemistry 224, 261.CrossRefGoogle Scholar
Exterkate, F. A. & Stadhouders, J. (1971). Netherlands Milk and Dairy Journal 25, 240.Google Scholar
French, C. S. & Milner, H. W. (1955). Methods in Enzymology 1, 64.CrossRefGoogle Scholar
Goldbarg, J. A. & Rutenburg, A. M. (1958). Cancer 11, 283.3.0.CO;2-8>CrossRefGoogle ScholarPubMed
Lee, H. J., LaRue, J. N. & Wilson, I. B. (1971). Analytical Biochemistry 41, 397.CrossRefGoogle Scholar
McKenzie, H. A. (1967). Advances in Protein Chemistry 22, 55.CrossRefGoogle Scholar
MacLeod, P. & Gordon, D. F. Jr (1961). Journal of Dairy Science 44, 237.CrossRefGoogle Scholar
Matheson, A. T. & Tattrie, B. L. (1964). Canadian Journal of Biochemistry 42, 95.CrossRefGoogle Scholar
Reiter, B. & Oram, J. D. (1962). Journal of Dairy Research 29, 63.Google Scholar
Sachs, D. H. & Painter, E. (1972). Science 175, 781.CrossRefGoogle Scholar
Sarid, S., Berger, A. & Katchalski, E. (1962). Journal of Biological Chemistry 237, 2207.CrossRefGoogle Scholar
Sørhaug, T. & Solberg, P. (1972). Journal of Dairy Science 55, 675.Google Scholar
Sullivan, J. J. & Jago, G. R. (1970). Australian Journal of Dairy Technology 25, 141.Google Scholar
Sullivan, J. J. & Jago, G. R. (1972). Australian Journal of Dairy Technology 27, 98.Google Scholar
Sullivan, J. J., Kieseker, F. G. & Jago, G. R. (1971). Australian Journal of Dairy Technology 26, 111.Google Scholar
Sullivan, J. J., Mou, L., Rood, J. I. & Jago, G. R. (1973). Australian Journal of Dairy Technology 28, 20.Google Scholar
Vanderheiden, G. J., Fairchild, A. C. & Jago, G. R. (1970). Applied Microbiology 19, 875.CrossRefGoogle Scholar
Van Der Zant, W. C. & Nelson, F. E. (1954). Journal of Dairy Science 37, 795.CrossRefGoogle Scholar
Yaron, A. & Mlynar, D. (1968). Biochemical and Biophysical Research Communications 32, 658.CrossRefGoogle Scholar