Esterification by rat liver microsomes of retinol bound to cellular retinol-binding protein.
نویسندگان
چکیده
منابع مشابه
Acyl-CoA-independent esterification of retinol bound to cellular retinol-binding protein (type II) by microsomes from rat small intestine.
Cellular retinol-binding protein (type II) (CRBP(II)), a newly described retinol-binding protein, is present in the small intestinal absorptive cell at high levels. Retinol (vitamin A alcohol) presented as a complex with CRBP(II) was found here to be esterified by microsomal preparations from rat small intestinal mucosa. The esterification observed utilized an endogenous acyl donor(s) and produ...
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To explore the nature of retinyl ester synthesis by liver microsomes, membranes prepared from rat or cat liver were incubated under various conditions with [3H] retinol dispersed in dimethyl sulfoxide. When [3H]retinol, buffer, and microsomes were incubated together (basal conditions), some [3H]retinol esterification was consistently observed. However, the rate of esterification could be increa...
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Because vitamin A in milk is largely present as esterified retinol while blood plasma predominantly contains unesterified retinol, experiments were conducted to determine whether membranes from the lactating mammary gland are able to synthesize retinyl esters in vitro. When microsomes from rats lactating for 7 to 14 days were incubated with [(3)H]retinol dispersed in dimethylsulfoxide, some [(3...
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Studies were conducted to explore the effects of colchicine on the secretion and metabolism of retinol-binding protein (RBP) by the liver. In the vitamin A-deficient rat, the rate of secretion of RBP from the liver into the serum is greatly reduced, and RBP accumulates in the liver. Injection of retinol (dispersed in a 20% Tween 40 solution) into deficient rats stimulated a rapid secretion of R...
متن کاملBinding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics.
The structure and backbone dynamics of rat holo cellular retinol-binding protein II (holo-CRBP II) in solution has been determined by multidimensional NMR. The final structure ensemble was based on 3980 distance and 30 dihedral angle restraints, and was calculated using metric matrix distance geometry with pairwise Gaussian metrization followed by simulated annealing. The average RMS deviation ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)37340-x