Partial purification of fatty-acid binding protein by ammonium sulphate fractionation.

Archives internationales de physiologie et de biochimie 08/1983; 91(2):103-8. DOI: 10.3109/13813458309078583
Source: PubMed

ABSTRACT By fractionation of rat liver cytosol with 70% saturation ammonium sulphate, a soluble fraction showing high affinity for oleic acid was obtained. The binding of oleic acid to this fraction was inhibited by flavaspidic acid. The molecular weight of the main protein present in this fraction was 12 000 as determined by SDS-poly-acrylamide-gel electrophoresis. This soluble fraction stimulated the transfer of oleic acid from microsomes to phosphatidylcholine liposomes as demonstrated by a transfer assay in vitro. The behaviour of this fraction is similar to that described for fatty-acid binding protein.

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    ABSTRACT: The palmitic acid binding capacity of cytosolic proteins in three preparations obtained by differential scraping of bovine intestinal mucosa were compared. The data indicated that the palmitic acid binding activities depended on the position that the cells occupied along the crypt-villus axis, as shown from the level of alkaline phosphatase activity. Proteins with palmitate binding properties in the high- and low-molecular-weight cytosolic proteins in the villus zone bound 1.24 +/- 0.41 and 1.54 +/- 0.16 pmol palminate/micrograms protein respectively. The binding decreased to 0.50 +/- 0.25 and 1.10 +/- 0.23 pmol palmitate/micrograms for the proteins in the crypt zone. Ammonium sulphate fractionation and gel filtration chromatography indicated that the low-molecular-weight cytosolic proteins obtained from light mucosal scrapings contained the highest palmitate binding activity. These results suggest that the cytosolic proteins located in the villus zone may play a role in the absorption of fatty acids.
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