Document Detail

Comparison of plasma membrane FABP and mitochondrial isoform of aspartate aminotransferase from rat liver.
MedLine Citation:
PMID:  8238519     Owner:  NLM     Status:  MEDLINE    
A relationship between plasma membrane fatty acid binding protein (FABPpm), a putative membrane transporter for long-chain fatty acids, and the mitochondrial isoform of aspartate aminotransferase (m-AspAT) has been reported. Accordingly, we have compared the chemical and immunological properties of rat liver m-AspAT with those of rat liver FABPpm isolated by two procedures: 1) detergent solubilization of the membranes followed by purification via fatty acid affinity chromatography (FABP-1) or 2) salt extraction of the membranes and subsequent purification by high-performance liquid chromatography (HPLC; FABP-2). Comparison of the three protein preparations revealed no differences with respect to NH2-terminal amino acid sequence, amino acid composition, peptides from tryptic digests, AspAT enzymatic activity, isoelectric point, mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), retention on five different HPLC columns, and immunoprecipitation and immunoblotting of SDS-PAGE separated proteins with polyclonal antisera. Examination of the proteins by nondenaturing PAGE showed a consistent second band in FABP-1 and FABP-2 not always present in m-AspAT. However, whenever present, this band was immunoreactive with antibodies to both m-AspAT and FABP-1. Hence, FABP-1 and FABP-2 are indistinguishable from one another. They are also at least closely related, if not identical, to m-AspAT.
D D Stump; S L Zhou; P D Berk
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of physiology     Volume:  265     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1993 Nov 
Date Detail:
Created Date:  1993-12-22     Completed Date:  1993-12-22     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  G894-902     Citation Subset:  IM    
Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029.
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MeSH Terms
Amino Acid Sequence
Aspartate Aminotransferases / chemistry,  isolation & purification*
Blotting, Western
Carrier Proteins / chemistry,  isolation & purification*
Cell Membrane / enzymology,  metabolism
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Fatty Acid-Binding Proteins
Fatty Acids / metabolism
Isoenzymes / chemistry,  isolation & purification*
Liver / enzymology,  metabolism*
Mitochondria, Liver / enzymology*
Molecular Sequence Data
Molecular Weight
Neoplasm Proteins*
Nerve Tissue Proteins*
Peptide Fragments / chemistry,  isolation & purification
Rats, Sprague-Dawley
Sequence Homology, Amino Acid
Grant Support
Reg. No./Substance:
0/Carrier Proteins; 0/Fabp1 protein, mouse; 0/Fabp1 protein, rat; 0/Fabp2 protein, mouse; 0/Fabp2 protein, rat; 0/Fabp7 protein, rat; 0/Fatty Acid-Binding Proteins; 0/Fatty Acids; 0/Isoenzymes; 0/Neoplasm Proteins; 0/Nerve Tissue Proteins; 0/Peptide Fragments; EC Aminotransferases

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