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Bartetzko, N; Lezius, AG; Spener, F.
Isoforms of fatty-acid-binding protein in bovine heart are coded by distinct mRNA.
Eur J Biochem. 1993; 215(3):555-559 Doi: 10.1111/j.1432-1033.1993.tb18065.x
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Co-authors Med Uni Graz: Spener Friedrich
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Abstract:: In the course of our studies on structure/function relationships of fatty-acid-binding proteins, we reported earlier that the two isoforms of the 15-kDa cardiac fatty-acid-binding protein (cFABP) from bovine heart only differ in one position; Asn98 in pI 5.1-cFABP; Asp98 in pI 4.9-cFABP [Unterberg, C., Börchers, T., Højrup, P., Knudsen, J. and Spener, F. (1990) J. Biol. Chem. 265, 16,255-16,261]. In the present study, we elucidate the origin for this heterogeneity. Isoelectric focusing analysis of immunoprecipitated in vitro translation products from total mRNA and positive-hybrid-selected cFABP/mRNA revealed two L-[35S]methionine-labeled proteins corresponding to pI 5.1-cFABP and pI 4.9-cFABP. In a control experiment, recombinant mRNA derived from cDNA encoding pI 5.1-cFABP was translated and produced only pI 5.1-cFABP as shown by isoelectric focusing of the translation products. We could observe co-translational acetylation but not post-translational deamidation of the cFABP isoforms. Taken together, our results demonstrate that the isoforms of cardiac fatty-acid-binding protein found in bovine heart are coded by distinct mRNA species.
Find related publications in this database (using NLM MeSH Indexing): Amides - metabolism; Amino Acid Sequence -; Animals -; Asparagine - metabolism; Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism; Cattle -; Fatty Acid-Binding Proteins -; Fatty Acids - metabolism; Molecular Sequence Data -; Myocardium - metabolism; Neoplasm Proteins -; Protein Biosynthesis -; RNA, Messenger - metabolism