Evidence for the lack of classical secretory phospholipase A2 in guinea-pig pancreas

• Published in: Biochimica et biophysica acta Vol. 666; no. 1; p. 72
• Main Authors: Fauvel, J, Bonnefis, M J, Chap, H, Thouvenot, J P, Douste-Blazy, L
• Format: Journal Article
• Language: English
• Published: Netherlands 23-10-1981
• Subjects: Animals; Cytoplasmic Granules - enzymology; Enzyme Activation; Guinea Pigs; Hot Temperature; Lipase - metabolism; Lysophospholipase - metabolism; Microscopy, Electron; Pancreas - enzymology; Phospholipases - metabolism; Phospholipases A - metabolism; Phospholipases A1; Phospholipases A2; Phospholipids - metabolism; Substrate Specificity; Trypsin - metabolism
• ISSN: 0006-3002
• DOI: 10.1016/0005-2760(81)90092-8

Several lipolytic enzymes from guinea-pig pancreas have been determined in a soluble extract and in a purified zymogen granule fractions. The positional specificity of phospholipolytic enzymes was detected using phospholipids bearing various radioactive labels. It is shown that guinea-pig pancreatic extracts are able to release both fatty acids from phosphatidylcholine, but with more efficiency towards the fatty acid occupying the 1-position of sn-glycerol. Evidence is given that guinea-pig pancreas lacks the classical secretory phospholipase A2 and that phospholipid digestion is achieved through the sequential action of phospholipase A1 and lysophospholipase.