Title : Fatty acyl CoA-dependent and -independent retinol esterification by rat liver and lactating mammary gland microsomes.

Pub. Date : 1991 Aug 1

PMID : 1898045






4 Functional Relationships(s)
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1 Retinol bound to cellular retinol-binding protein (CRBP) or dispersed in solvent was esterified in a fatty acyl CoA-independent, PMSF-sensitive reaction, consistent with lecithin:retinol acyltransferase (LRAT) activity. Vitamin A lecithin retinol acyltransferase Rattus norvegicus
2 Retinol bound to cellular retinol-binding protein (CRBP) or dispersed in solvent was esterified in a fatty acyl CoA-independent, PMSF-sensitive reaction, consistent with lecithin:retinol acyltransferase (LRAT) activity. Vitamin A lecithin retinol acyltransferase Rattus norvegicus
3 LRAT activity exhibited the same Km (2 microM retinol) between tissues but a higher Vmax in liver as compared to that in mammary gland (47 vs 8 pmol/min/mg microsome protein, respectively). Vitamin A lecithin retinol acyltransferase Rattus norvegicus
4 Thus, when substrate was near or below Km, retinol esterification occurred predominantly by LRAT in the liver and ARAT in the mammary gland, respectively. Vitamin A lecithin retinol acyltransferase Rattus norvegicus