乳酸链球菌细胞表面蛋白酶的定位
Localization of proteinase(s) near the cell surface of Streptococcus lactis.
作者信息
Thomas T D, Jarvis B D, Skipper N A
出版信息
J Bacteriol. 1974 May;118(2):329-33. doi: 10.1128/jb.118.2.329-333.1974.
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.
摘要
有两条标准表明，乳酸链球菌的大多数蛋白酶定位于细胞壁。（i）完整细胞与高分子量底物一起孵育时具有蛋白酶活性。（ii）在仅导致1%的细胞内酶醛缩酶和甘油醛-3-磷酸脱氢酶释放的条件下，原生质球形成过程中大部分细胞结合的蛋白酶活性被释放。以酪蛋白为底物时，溶解的细胞壁、质膜和细胞质部分分别含有总蛋白酶活性的84%、0%和16%。本文讨论了这种生物体中表面结合蛋白酶的生理作用。
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