Evidence for the lack of classical secretory phospholipase A2 in guinea-pig pancreas.
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.
D000818:Animals; D003594:Cytoplasmic Granules / Q000201:enzymology*; D004789:Enzyme Activation; D006168:Guinea Pigs; D006358:Hot Temperature; D008049:Lipase / Q000378:metabolism; D008245:Lysophospholipase / Q000378:metabolism; D008854:Microscopy, Electron; D010179:Pancreas / Q000201:enzymology*; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054466:Phospholipases A1; D054467:Phospholipases A2; D010743:Phospholipids / Q000378:metabolism*; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism
D010743:Phospholipids; D010740:Phospholipases; D008049:Lipase; D010741:Phospholipases A; D054466:Phospholipases A1; D054467:Phospholipases A2; D008245:Lysophospholipase; D014357:Trypsin