Wallinder_1982_Biochim.Biophys.Acta_711_107

Lipoprotein lipase was purified from guinea pig milk by chromatography on heparin-Sepharose followed by chromatography on an immobilized preparation of heparin that had been N-desulphated and then acetylated. This second step was necessary to separate a plasma protein, presumably antithrombin, from the lipase. The guinea pig enzyme turned out to be quite similar to lipoprotein lipase from bovine milk with respect to composition and molecular size. Furthermore, the specific activities and the dose-response relations for activation by apolipoprotein C-II were quite similar for the two enzymes. Antibodies raised against the guinea pig milk enzyme inhibited not only this enzyme but also the lipoprotein lipase activity in post-heparin plasma and in homogenates from adipose tissue and heart.