Positional Specificity of Lipoprotein Lipase
نویسندگان
چکیده
منابع مشابه
Positional specificity of lipoprotein lipase.
The stereochemical course of hydrolysis of radioactive triolein was determined using lipoprotein lipase of cow’s milk and rat postheparin plasma. [3H]Glycerol trioleate or glycerol [lJ4C]trioleate was emulsified with total egg yolk lipids to provide 0.2 to 2.5 PCi of 3H or 0.03 PCi of 14C per PM substrate. The hydrolysis products were isolated at 1 to 45 min and free fatty acids and the various...
متن کاملThe fatty acid and positional specificities of lipoprotein lipase.
Lipoprotein lipase has been identified in extracts of adipose tissue and heart and seems to be identical to the lipase that appears in plasma after the injection of a polyanion (cf. 1,2). The most unique characteristic of this lipase is its specificity for triglycerides in the form of a natural or synthetic lipoprotein complex. This paper describes investigations on the specificity of lipoprote...
متن کاملPositional specificity of hormone-sensitive lipase from rat adipose tissue.
Hormone-sensitive lipase, purified from rat adipose tissue (Fredrikson, G., Strålfors, P., Nilsson, N. O., and Belfrage, P. (1981) J. Biol. Chem. 256, 6311-6320), has been incubated with tri-, di-, and monooleoyl[3H]glycerol, and the acylglycerol reaction products were isolated by thin layer chromatography on silicic acid, impregnated with boric acid. Trioleoylglycerol was hydrolyzed with the i...
متن کاملSpecificity of lipoprotein lipase binding to endothelial cells.
Lipoprotein lipase (LPL) hydrolyzes circulating lipoprotein triglyceride molecules while it is associated with the luminal surface of capillary endothelial cells. The precise molecular mechanism by which LPL attaches to these cells is unknown. LPL and a number of other molecules, including growth factors and clotting factors, bind to heparin-affinity gels and are eluted using high concentration...
متن کاملSubstrate specificity of lipoprotein lipase and endothelial lipase: studies of lid chimeras.
The triglyceride (TG) lipase gene subfamily, consisting of LPL, HL, and endothelial lipase (EL), plays a central role in plasma lipoprotein metabolism. Compared with LPL and HL, EL is relatively more active as a phospholipase than as a TG lipase. The amino acid loop or "lid" covering the catalytic site has been implicated as the basis for the difference in substrate specificity between HL and L...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44705-4