Neutral and acid retinyl ester hydrolases associated with rat liver microsomes: relationships to microsomal cholesteryl ester hydrolases
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چکیده
منابع مشابه
Neutral and acid retinyl ester hydrolases associated with rat liver microsomes: relationships to microsomal cholesteryl ester hydrolases.
We recently reported the presence of a neutral, bile salt-independent retinyl ester hydrolase (REH) activity in rat liver microsomes and showed that it was distinct from the previously studied bile salt-dependent REH and from nonspecific carboxylesterases (Harrison, E. H., and M. Z. Gad. 1989. J. Biol. Chem. 264: 17142-17147). We have now further characterized the hydrolysis of retinyl esters b...
متن کاملHepatic Retinyl Ester Hydrolases and the Mobilization of Retinyl Ester Stores
For mammals, vitamin A (retinol and metabolites) is an essential micronutrient that is required for the maintenance of life. Mammals cannot synthesize vitamin A but have to obtain it from their diet. Resorbed dietary vitamin A is stored in large quantities in the form of retinyl esters (REs) in cytosolic lipid droplets of cells to ensure a constant supply of the body. The largest quantities of ...
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Homogenates of bovine neuroretina and retinal pigment epithelium (RPE) were incubated with 11-cis and all-trans retinyl palmitate to study retinyl ester hydrolysis. The highest activity was found in RPE when 11-cis retinyl palmitate served as substrate (Km = 7.8 microM and Vmax = 44.8 pmol/min/mg). This retinyl ester hydrolase (REH) had an optimum activity at acidic pH (pH 5), which is in contr...
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An attempt was made to establish the number and characteristics of the enzymes in pancreatic juice that hydrolyze nitrogen- and phosphorus-free esters of fatty acids. For this purpose model compounds were hydrolyzed by lyophilized rat pancreatic juice under conditions that accelerated or inhibited the reactions. Although it is not established with certainty, it is suggested that three enzymes a...
متن کاملA triglyceride and cholesteryl ester transfer protein associated with liver microsomes.
An intracellular protein accelerates the transfer of triglyceride and cholesteryl ester. The fraction of phospholipid transferred was much less than for the less polar lipids. A rich source of this activity was obtained from low ionic strength washes of liver microsomes. The protein was partially purified by column chromatography on Bio-Gel A-5m and hydroxylapatite. The elution position of the ...
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ژورنال
عنوان ژورنال: Journal of Lipid Research
سال: 1991
ISSN: 0022-2275
DOI: 10.1016/s0022-2275(20)42056-5