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Positional Specificity of Lipoprotein Lipase

From the ¹ From the Banting and Best Department of Medical Research, Charles H. Best Institute, University of Toronto, Toronto, Ontario, Canada

The stereochemical course of hydrolysis of radioactive triolein was determined using lipoprotein lipase of cow's milk and rat postheparin plasma. [³H]Glycerol trioleate or glycerol [1-¹⁴C]trioleate was emulsified with total egg yolk lipids to provide 0.2 to 2.5 µCi of ³H or 0.03 µCi of ¹⁴C per µm substrate. The hydrolysis products were isolated at 1 to 45 min and free fatty acids and the various positional isomers of mono- and diglycerides were resolved by thin layer chromatography. In a total yield of 0.03 to 0.16 µmole of diglyceride, 9 to 30% was 1,3- and 70 to 91%, 1,2-(2,3-)diglyceride. The 2,3-isomer was 73 to 96% of the latter. The yield of free fatty acids and monoglycerides varied with the length of incubation. In 15 of 17 determinations, the 1-(3-)isomer accounted for 51 to 87% of the monoglyceride. It is suggested that lipoprotein lipase attacks preferentially position 1 in sn-glycerides and follows it by hydrolysis of the positions 2 and 3. An intermediate formation of 2,3-diglycerides during lipoprotein lipase hydrolysis may be important in avoiding stimulation of triglyceride and phospholipid biosynthesis which proceed via 1,2-diglycerides.

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