|Title||Isolation and partial characterization of plasma membrane fatty acid binding proteins from myocardium and adipose tissue and their relationship to analogous proteins in liver and gut.|
|Publication Type||Journal Article|
|Year of Publication||1987|
|Authors||Potter BJ, Stump D, Schwieterman W, Sorrentino D, Jacobs LN, Kiang CL, Rand JH, Berk PD|
|Journal||Biochem Biophys Res Commun|
|Date Published||1987 Nov 13|
|Keywords||Adipose Tissue, Animals, Carrier Proteins, Cell Membrane, Chromatography, Affinity, Fatty Acid-Binding Protein 7, Fatty Acid-Binding Proteins, Fatty Acids, Immunodiffusion, Isoelectric Point, Jejunum, Liver, Male, Membrane Proteins, Molecular Weight, Myocardium, Neoplasm Proteins, Nerve Tissue Proteins, Rats|
We describe a general method for isolating a class of 40 kDa plasma membrane fatty acid binding proteins which have been identified previously only in rat liver and jejunum. Proteins extracted with 2 M salt from rat adipocyte and cardiac myocyte plasma membranes were subjected to preparative isoelectric focusing. Fractions with pI's greater than or equal to 9.0 were further purified by oleate-agarose affinity chromatography and HPLC. Each tissue yielded a single 40 kDa protein which co-chromatographed with [3H]-oleate on gel permeation HPLC, and reacted on Western blots with an antibody to the corresponding hepatic membrane protein. Related plasma membrane fatty acid binding proteins have now been isolated from each of the major sites of fatty acid transport.
|Alternate Journal||Biochem Biophys Res Commun|
|Grant List||AA-06860 / AA / NIAAA NIH HHS / United States |
AM 26438 / AM / NIADDK NIH HHS / United States
Jacob H. Rand, M.D.