Properties of salt-resistant lipase and lipoprotein lipase purified from human post-heparin plasma.
Lipoprotein lipase and salt-resistant lipase were isolated from human post-heparin plasma. The proteins of human post-plasma lipoprotein lipase and salt-resistant lipase were identified and demonstrated to be immunologically different. Significant differences between the two enzymes in their relative amino acid composition were demonstrated, which indicates that the two enzymes are different proteins. When analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the enzymes seemed to have monomer molecular weights similar to that of lipoprotein lipase purified from bovine milk.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin; D006801:Humans; D005779:Immunodiffusion; D007074:Immunoglobulin G; D008049:Lipase / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D008071:Lipoprotein Lipase / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D008892:Milk / Q000201:enzymology; D012965:Sodium Chloride
D000596:Amino Acids; D007074:Immunoglobulin G; D012965:Sodium Chloride; D006493:Heparin; D008049:Lipase; D008071:Lipoprotein Lipase