NDLI: Plasma membrane fatty acid-binding protein and mitochondrial glutamic-oxaloacetic transaminase of rat liver are related.

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Plasma membrane fatty acid-binding protein and mitochondrial glutamic-oxaloacetic transaminase of rat liver are related.

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Plasma membrane fatty acid-binding protein and mitochondrial glutamic-oxaloacetic transaminase of rat liver are related.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sorrentino, D. Wada, H. Potter, B. J. Stump, D. Thung, S. Kiang, C. L. Zhou, S. L. Berk, P. D. Horio, Y. Isola, L. M.
Description	Author Affiliation: Berk PD ( Department of Medicine (Hepatic Research Group), Mount Sinai School of Medicine, New York, NY 10029.);
Abstract	The hepatic plasma membrane fatty acid-binding protein (h-FABPPM) and the mitochondrial isoenzyme of glutamic-oxaloacetic transaminase (mGOT) of rat liver have similar amino acid compositions and identical amino acid sequences for residues 3-24. Both proteins migrate with an apparent molecular mass of 43 kDa on SDS/polyacrylamide gel electrophoresis, have a similar pattern of basic charge isomers on isoelectric focusing, are eluted similarly from four different high-performance liquid chromatographic columns, have absorption maxima at 435 nm under acid conditions and 354 nm at pH 8.3, and bind oleate with a Ka approximately 1.2-1.4 x 10(7) M-1. Sinusoidally enriched liver plasma membranes and purified h-FABPPM have GOT enzymatic activity; the relative specific activities (units/mg) of the membranes and purified protein suggest that h-FABPPM constitutes 1-2% of plasma membrane protein in the rat hepatocyte. Monospecific rabbit antiserum against h-FABPPM reacts on Western blotting with mGOT, and vice versa. Antisera against both proteins produce plasma membrane immunofluorescence in rat hepatocytes and selectively inhibit the hepatocellular uptake of [3H]oleate but not that of [35S]sulfobromophthalein or [14C]taurocholate. The inhibition of oleate uptake produced by anti-h-FABPPM can be eliminated by preincubation of the antiserum with mGOT; similarly, the plasma membrane immunofluorescence produced by either antiserum can be eliminated by preincubation with the other antigen. These data suggest that h-FABPPM and mGOT are closely related.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aspartate Aminotransferases Genetics Carrier Proteins Liver Metabolism Mitochondria, Liver Enzymology Neoplasm Proteins Nerve Tissue Proteins Amino Acid Sequence Animals Antibodies, Monoclonal Isolation & Purification Blotting, Western Cell Membrane Cells, Cultured Chromatography, High Pressure Liquid Fatty Acid-Binding Proteins Fatty Acids Fluorescent Antibody Technique Kinetics Ultrastructure Microscopy, Electron Oleic Acid Oleic Acids Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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