Properties of purified bovine milk lipoprotein lipase.
Lipoprotein lipase has been purified from bovine milk by affinity chromatography on Sepharose containing covalently linked heparin. In addition to an enzyme eluted by salt, further activity could be eluted with detergent. Rechromatography experiments suggested that the two activities were due to the same enzyme. This assumption was further verified by several other criteria as follows: (a) both require a serum activator, (b) their apparent molecular weights (55 000), their amino acid compositions and amino sugar contents were similar and (c) they had identical immunological reactivities. Thus, the enzyme appears to be bound to the heparin-Sepharose matrix by both salt-reversed and detergent-reversed interactions. Sodium deoxycholate stimulated the activity eluted by high salt, but had no effect on the detergent-eluted enzyme.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D003840:Deoxycholic Acid / Q000494:pharmacology; D005260:Female; D005688:Galactosamine / Q000032:analysis; D005944:Glucosamine / Q000032:analysis; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000302:isolation & purification / Q000378:metabolism; D008892:Milk / Q000201:enzymology*
D000596:Amino Acids; D003840:Deoxycholic Acid; D005688:Galactosamine; D008071:Lipoprotein Lipase; D005944:Glucosamine