Detection and partial characterization of lipoprotein lipase in bovine aorta.
Extracts of acetone-ether powders of bovine thoracic aorta contain lipase activity which has an alkaline pH maximum (7.8-8.4) and is stimulated 4-10-fold by adding serum or isolated apolipoprotein-glutamate to the assay mixture. Serum activation is completely reversed by isolated apolipoprotein-serine or apolipoprotein-alanine. Lipolysis is strongly inhibited by NaCl (0.5 M) and protamine sulfate (1 mg/ml) and partially inhibited by heparin. Based on these characteristics, the lipase is identified as lipoprotein lipase.
D000818:Animals; D001013:Aorta, Thoracic / Q000201:enzymology*; D001059:Apoproteins / Q000494:pharmacology; D001769:Blood; D002417:Cattle; D004789:Enzyme Activation; D006493:Heparin / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008071:Lipoprotein Lipase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008074:Lipoproteins / Q000494:pharmacology; D011479:Protamines / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology
D001059:Apoproteins; D008074:Lipoproteins; D011479:Protamines; D012965:Sodium Chloride; D006493:Heparin; D008071:Lipoprotein Lipase