Lipoprotein lipase of sheep and rat adipose tissues.

Lipoprotein lipase preparations were obtained by aqueous extraction of various tissues from sheep and rats. Preparations having high activity towards serum-activated triolein emulsions were obtained from actively growing sheep, provided that the tissue was maintained at 37 degrees C throughout the extraction procedure. Activity of lipoprotein lipase from sheep adipose tissue, like that from the rat, was dependent upon the presence of serum in the reaction mixture, and was optimal at pH 8-9. Inhibition of sheep adipose tissue preparations by protamine sulfate (1 mg/ml) and 0.6 M NaCl was similar to that found for rat adipose tissue preparations. The affinity of the lipoprotein lipase preparation for the activated substrate from sheep and rat adipose tissue was, however, markedly different; sheep preparations being activated at much lower substrate concentrations (Km 0.43 mM) than rat preparations (Km greater than 5 mM). These findings, confirmed with acetone-ether preparations of lipoprotein lipase, indicate that the enzyme from sheep adipose tissue has a greater potential to remove triacylglycerol from the plasma. This could result in a greater deposition of fat in the tissue.