Abstract
The binding of [3H]oleic acid and [3H]palmitic acid to the low molecular weight fatty acid binding proteins present in the cytosols of rat liver and heart was studied. Both fatty acids were bound by Z protein of liver, whereas only oleic acid was bound by the fraction of heart that contains the fatty acid binding protein. However, after delipidation of heart cytosolic proteins with butanol, the binding of palmitic acid to the fatty acid binding protein was detected. In contrast to a published report (Gloster, J., and Harris, P. (1977) Biochem. Biophys. Res. Commun. 74, 506-513), oleic acid was not bound by rat heart or bovine heart myoglobin. Both rat heart fatty acid binding protein and rat liver Z protein were purified to homogeneity or near homogeneity. On polyacrylamide gel electrophoresis under nondenaturing conditions, liver Z protein gave rise to three bands, none of which was identical with the single band due to heart fatty acid binding protein. Rabbit antibodies to rat liver Z protein were used to demonstrate that the purified fatty acid binding protein from rat liver (Z protein) and rat heart are immunologically unrelated and that no Z protein is present in rat heart cytosol. Taken together, these observations lead to the conclusion that the low molecular weight fatty acid binding proteins from rat liver and heart are different proteins.
Highlights
From the Departmentof Chemistry, City College of the City University of New York, New York, New York 10031
Rabbit antibodies to rat liver Z protein were used to demonstrate that the purified fatty acid binding protein from rat liver (Z protein) and rat heart are immunologically unrelated and that no Z protein is present in rat heart cytosol
The existence oflow molecular weight fatty acid binding proteins in the cytosols of various animal tissues was first reported by Ockner et al [1].The best characterizedof these binding proteins is that from rat liver which appears to be identicalwiththeanion-bindingprotein or Z protein described by Levi et al [2]
Summary
From the Departmentof Chemistry, City College of the City University of New York, New York, New York 10031. Tothe resulting solution of cytosolic proteins (1.4 g) were added 4 nmol of [9,10-3H]oleic acid (9.5 Ci/mmol) dissolved in 4 pl of ethanol This sample was chromatographed on a Sephadex G-75 column (4 x 42 cm) equilibratedwith 10 mM sodium acetate (pH 5). Thceolumn was developed with a linear gradient made up of 50 ml each of 10 mM sodium acetate (pH5) and 0.2 M sodium acetate (pH5).The fractions containing most of the radioactivity were pooled and concentrated in an Amicon concentrator (PM-10 membrane) to yield 7.5 mg of Z protein. The fractions containing most of the radioactivity were pooled and concentratedin an Amicon concentrator(UM-2membrane).The resulting 2.7 mg of protein were applied to a DEAE-cellulose column (0.9 X 7 cm) equilibrated with 10mM Tris phosphate (pH 8.3). IO - brane) to yield 0.11 mg of pure fatty acid binding protein
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