Stereospecificity of lipases. Enzymic hydrolysis of enantiomeric alkyl diacylglycerols by lipoprotein lipase, lingual lipase and pancreatic lipase

Hydrolysis of diacylglycerols by lipoprotein lipase.

Enantiomeric diacylglycerols were emulsified, mole for mole, with lyso(1-acyl) lecithin and were hydrolyzed with lipoprotein lipase in NH4Cl-beef serum albumin buffer at pH 8.6 after a brief incubation with delipidated rat serum. The enzyme was prepared from lyophilized and dialyzed bovine skim milk in a 4 percent solution. The course of hydrolysis for each set of enantiomers was determined by ...

Chimeras of Hepatic Lipase and Lipoprotein Lipase

Chimeric molecules between human lipoprotein lipase (LPL) and rat hepatic lipase (HL) were used to identify structural elements responsible for functional differences. Based on the close sequence homology with pancreatic lipase, both LPL and HL are believed to have a two-domain structure composed of an aminoterminal (NHz-terminal) domain containing the catalytic Ser-His-Asp triad and a smaller ...

Studies of fat lipolysis by post-heparin human plasma lipoprotein lipase and by human pancreatic lipase.

The Phosphate Ion and Hydrolysis by Pancreatic Lipase

The equation, (activity of enzyme) (pPO(4))(n) = K, has been investigated and has been shown to have only a limited application to the effect of the phosphate ion on the hydrolytic activity of pancreatic lipase. The deviations observed are ascribed to the effect of certain factors on the stability of the enzyme.

Rat Lingual Lipase

The lingual serous glands of rat tongue secrete a potent lipase that hydrolyzes long chain triglycerides. The characteristics of this lipase were studied in preparations of lingual glands from Sprague-Dawley rats. Lipase activity was measured by the release of free fatty acids from emulsified tri[3H]oleate. Lipase activity in the 100,000 x g supernatant of lingual serous gland homogenate was ex...