The action of phospholipase A on purified phospholipids, plasma and tissue preparations

作者：Ibrahim Sa, Hazel Sanders, RHS THOMPSON · 发表于：Biochemical Journal · 年份：1964 · DOI：10.1042/bj0930588 · 被引用次数：52 · 研究领域：Metabolism and Genetic Disorders、Amino Acid Enzymes and Metabolism、Muscle metabolism and nutrition

Earlier work in this Laboratory on the action of phospholipase A in aqueous systems indicated that the phospholipase A (phosphatide acyl-hydrolase, EC 3.1.1.4) in human pancreas, unlike the enzyme in snake venom from Cottonmouth moccasin (Agkistrodon piscivorus piscivoru8), does not hydro- lyse purified ovolecithin readily in the system 2,4,6- collidine-diethyl ether described by Magee & Thompson (1960).Nor does it readily attack purified ovolecithin in a glycylglycine buffer system unless sodium deoxycholate is present (Magee, Gallai-Hatchard, Sanders & Thompson, 1962).Vogel & Zieve (1960), working with the phospholipase A of human duodenal contents, also obtained evidence of activation of the hydrolysis of lecithin by deoxycholate.In unpublished work, however, H. Sanders & R. H. S. Thompson found that the pancreatic