PHOSPHOLIPID-METABOLISM IN NEISSERIA-GONORRHOEAE - PHOSPHOLIPID HYDROLYSIS IN NONGROWING CELLS

被引:8
作者
CACCIAPUOTI, AF [1 ]
WEGENER, WS [1 ]
MORSE, SA [1 ]
机构
[1] UNIV OREGON, HLTH SCI CTR, DEPT MICROBIOL & IMMUNOL, PORTLAND, OR 97201 USA
关键词
D O I
10.1007/BF02533897
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hydrolysis of cell envelope phospholipids was demonstrated in cells of both autolytic and nonautolytic strains of Neisseria gonorrhoeae that were labeled during growth in the presence of [3H] acetate. The label incorporated into the cellular phospholipids was located exclusively in the fatty acid acyl side chains. Labeled cells were incubated for 2 hr in N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid buffer, pH 8.5, containing various additions, and then examined for distribution of3H in lipids. Ca++ selectively stimulated the deacylation of phosphatidylethanolamine (PE), whereas Mn++ stimulated the deacylation of phosphatidylglycerol (PG). Hydrolysis of phosphatidylethanolamine by phospholipase A was accompanied by the accumulation of lysophosphatidylethanolamine (LPE) and free fatty acids in the cells. Free fatty acids accumulated to a greater extent than lysophosphatidylethanolamine, suggesting that the latter was further hydrolyzed to glycerophosphorylethanolamine (GPE) and free fatty acids by a lysophospholipase. Methanol, ethanol, propanol, and isopropanol, added at concentrations which inhibited growth by 50%, stimulated phospholipase A, but not lysophospholipase activity. Differences in heat inactivation, metal ion requirements, and pH optima suggested that phospholipase A activities with phosphatidylethanolamine or phosphatidylglycerol as substrate and lysophospholipase may be separate enzymes. © 1979 American Oil Chemists' Society.
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页码:718 / 726
页数:9
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