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Positional specificity of adipose tissue lipoprotein lipase
Author(s) -
NilssonEhle P.,
Garfinkel A. S.,
Schotz M. C.
Publication year - 1974
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532503
Subject(s) - lipoprotein lipase , adipose tissue , lipase , chemistry , biochemistry , chromatography , glycerol , lipidology , enzyme , hydrolysis , triglyceride , thin layer chromatography , triolein , lipoprotein , substrate (aquarium) , clinical chemistry , biology , cholesterol , ecology
Abstract 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 with 3 H in the glycerol moiety and with 14 C 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.