Abstract
A new alkaline lipase was detected in rat brain and its properties were compared with those of the well-characterized pancreatic lipase and pancreatic lipase-related protein 2. The activity of the alkaline lipase was determined using trioleoylglycerol emulsion at pH 8.0. Subcellular fractions were prepared from brain homogenates by differential centrifugation. Lipase activities of the cytosolic fraction (the supernatant obtained by differential centrifugation of 100,000g) were stimulated by addition of colipase and bile salts and inhibited by addition of an antibody against rat pancreatic lipase. The partially purified enzyme had an isoelectric point of pH 6.8, which was identical to that found for rat pancreatic lipase. The enzyme had interfacial activation and dependence on colipase in the presence of bile salts. The enzyme had no measurable phospholipase A activity. The band produced by the enzyme on SDS–polyacrylamide gel electrophoresis was identical to that of the rat pancreatic lipase when detected by immunoblotting analysis using an antibody against pancreatic lipase. These results show that pancreatic lipase such as alkaline lipase is in rat brain.
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