Highly purified lipoprotein lipase from bovine milk has been incubated with emulsified 1,3-dioleoyl-2-[1-14C]oleoyl-[3H]glycerol, and the reaction products have been separated by thin layer chromatography on silicic acid impregnated with boric acid. There was an appreciable accumulation of monoacylglycerol, preponderantly of the 2 configuration. The 1(3)-monoacylglycerol found must have been formed by isomerization from the 2 isomer. A small but constant amount of 1,2(2,3)-diacylglycerol was found among the reaction products, but no 1,3-diacylglycerol. In incubations of albumin-bound 1(3)-monooleoylglycerol and 2-monooleoylglycerol with the enzyme, glycerol was produced by hydrolysis of the 1(3) isomer exclusively. In the incubations with trioleoylglycerol substrate, glycerol thus must have been obtained by hydrolysis of 1(3)-monoacylglycerol formed by isomerization from the 2 isomer. The main reaction sequence was triacylglycerol → 1,2(2,3)-diacylglycerol → 2-monoacylglycerol ⇌ 1(3)-monoacylglycerol → glycerol. The enzyme thus has a specificity for position 1(3) of the acylglycerols.
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Nilsson‐Ehle et al. (1973) studied this question.