Affiliation:
1. New Zealand Dairy Research Institute, and Department of Microbiology and Genetics, Massey University, Palmerston North, New Zealand
Abstract
Two criteria suggest that most of the proteinase of
Streptococcus lactis
is localized in the cell wall. (i) Intact cells possess proteinase activity when incubated with a high-molecular-weight substrate. (ii) Most of the cell-bound proteinase activity is released during spheroplast formation under conditions which result in the release of only 1% of the intracellular enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase. The solubilized cell wall, plasma membrane, and cytoplasm fractions contained 84, 0, and 16%, respectively, of the total proteinase activity with casein as substrate. The physiological role of a surface-bound proteinase in this organism is discussed.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
84 articles.
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