Phylogeny of lipase specificity
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 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...
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 کاملAcyl-chain specificity of human milk bile-salt-activated lipase.
In order to probe the active-site structure of human milk bile-salt-activated lipase (BAL), the kinetics of the BAL-catalysed reaction were studied using monoesters as substrates. Among the fatty acyl chains, ranging from C8 to C16 of monoacylglycerols in a single equimolar assay mixture, there was a consistent trend of increased reactivity with decreased fatty-acyl-chain length for both the ba...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Lipids
سال: 1970
ISSN: 0024-4201,1558-9307
DOI: 10.1007/bf02532745