作者: Z Shen , D M Byers
DOI: 10.1128/JB.176.1.77-83.1994
关键词: Biochemistry 、 Phospholipid 、 Acylation 、 Myristic acid 、 Fatty acid 、 Vibrio harveyi 、 Acyl carrier protein 、 Biology 、 Gel electrophoresis 、 Sodium dodecyl sulfate
摘要: To study the involvement of acyl carrier protein (ACP) in metabolism exogenous fatty acids Vibrio harveyi, cultures were incubated minimal medium with [9,10-3H]myristic acid, and labeled proteins analyzed by gel electrophoresis. Labeled acyl-ACP was positively identified immunoprecipitation anti-V. harveyi ACP serum comigration standards [3H]beta-alanine-labeled bands on both sodium dodecyl sulfate- urea-polyacrylamide gels. Surprisingly, most label corresponded to acid chain lengths less than 14 carbons: C14, C12, C10, C8 represented 33, 40, 14, 8% total [3H]14:0-derived acyl-ACPs, respectively, a dark mutant (M17) V. which lacks myristoyl-ACP esterase activity; however, 14:0-ACP absent wild-type strain. 14:0- 12:0-ACP also predominant species complex medium. In contrast, short-chain acyl-ACPs ( or = C8) [3H]beta-alanine fivefold, while incorporation [3H]14:0 not affected, although shift shorter noted. Additional comigrated sulfate gels as lipopolysaccharide hydrolysis thin-layer chromatography. The levels [3H] 14:0 into 2 15%, that phospholipid 10 min. Our results indicate contrast situation Escherichia coli, can be activated intermediates after partial degradation effectively products (i.e., lipid A) require an donor.