Literature DB >> 235577

Pptidase activities in group N streptococci.

J J Sullivan, G R Jago, L Mou.   

Abstract

Several peptidase activites 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-beta-napthylamidase), 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.

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Year:  1975        PMID: 235577     DOI: 10.1017/s002202990001517x

Source DB:  PubMed          Journal:  J Dairy Res        ISSN: 0022-0299            Impact factor:   1.904


  3 in total

1.  Purification and Characterization of a Substrate-Size-Recognizing Metalloendopeptidase from Streptococcus cremoris H61.

Authors:  T R Yan; N Azuma; S Kaminogawa; K Yamauchi
Journal:  Appl Environ Microbiol       Date:  1987-10       Impact factor: 4.792

2.  Purification and Some Properties of a Membrane-Bound Aminopeptidase A from Streptococcus cremoris.

Authors:  F A Exterkate; G J de Veer
Journal:  Appl Environ Microbiol       Date:  1987-03       Impact factor: 4.792

Review 3.  Proteolytic systems in lactic acid bacteria.

Authors:  B A Law; J Kolstad
Journal:  Antonie Van Leeuwenhoek       Date:  1983-09       Impact factor: 2.271

  3 in total

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