Characterization of two triacylglycerol lipase activities in pig post-heparin plasma.
Two triacylglycerol lipase activities were characterized after partial purification from pig post-heparin plasma. These two lipase activities were eluted sequentially with a NaCl gradient from columns containing Sepharose with covalently linked heparin. The first lipase activity, which was eluted at 0.75M-NaCl, was not inhibited at 28 degrees C in the presence of 1M-NaCl and was not further activated by plasma apolipoproteins. The absence of this lipase activity from post-heparin plasma from hepatectomized pigs indicates that the liver plays a role in the synthesis of this enzyme. A second lipase activity, which was eluted at 1.2M-NaCl, was inhibited when assayed in the presence of 1.0M-NaCl and was activated 14-fold by an apolipoprotein isolated from human very-low-density lipoprotein. The characteristics are identical with those of lipoprotein lipase purified from pig adipose tissue.
D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D006493:Heparin / Q000494:pharmacology; D006498:Hepatectomy; D008049:Lipase / Q000097:blood*; D008071:Lipoprotein Lipase / Q000097:blood; D012965:Sodium Chloride / Q000494:pharmacology; D013552:Swine
D012965:Sodium Chloride; D006493:Heparin; D008049:Lipase; D008071:Lipoprotein Lipase