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The positional specificity of preparations of lipoprotein lipase derived from rat epididymal adipose tissue was investigated. The enzyme preparations were a crude extract of acetone powder of the whole tissue, partially purified lipoprotein lipase fractions a and b separated by gel chromatography from such an extract, and lipoprotein lipase activity eluted from adipose tissue into a medium by incubation with heparin in vitro. The enzyme preparations were incubated with triglyceride substrate labeled with3H in the glycerol moiety and with14C in the fatty acid esterified to the 2 position of the glycerol. The reaction products were separated by thin layer chromatography. All preparations preferentially hydrolyzed the 1(3) ester bonds of the tri‐ and diglycerides, indicating that, like lipoprotein lipase from other sources, the adipose tissue enzyme has a specificity for the 1(3) position.

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