RESUMEN
1. Two distinct fatty acid binding proteins (FABPs) were isolated and characterized from chicken duodenal mucosa. 2. Molecular weight, functional activity, immunospecificity, mRNA expression, and amino acid composition data for the 14 kDa chicken intestinal FABP was similar, yet not identical, to that of a previously isolated chicken liver FABP. 3. Bound fatty acids were shown to produce isoforms of the 14 kDa intestinal protein but not the larger molecular weight intestinal FABP.
Asunto(s)
Proteínas Portadoras/aislamiento & purificación , Pollos/metabolismo , Ácidos Grasos/metabolismo , Mucosa Intestinal/metabolismo , Aminoácidos/análisis , Animales , Northern Blotting , Proteínas Portadoras/análisis , Cromatografía en Gel , Cromatografía por Intercambio Iónico , Electroforesis en Gel de Poliacrilamida , Focalización Isoeléctrica , ARN/aislamiento & purificaciónRESUMEN
1. Fatty acid binding protein (FABP) was isolated from chicken liver cytosol. 2. Apparent molecular weight, pI, functional activity, and hybridization of a rat hFABP cDNA probe with chicken liver mRNA suggest that chicken liver FABP is structurally related to hepatic FABP (hFABP) previously isolated and characterized in the rat. 3. Fatty acids bound to liver FABP affect the electrophoretic nature of FABP. 4. Levels of liver FABP mRNA isolated from chickens at various stages of development parallel developmental alterations in lipid metabolism, being highest in day old chicks and laying hens versus juvenile birds.