Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Jagschies, G; Reers, M; Unterberg, C; Spener, F.
Bovine fatty acid binding proteins. Isolation and characterisation of two cardiac fatty acid binding proteins that are distinct from corresponding hepatic proteins.
Eur J Biochem. 1985; 152(3):537-545
Doi: 10.1111/j.1432-1033.1985.tb09229.x
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- Co-Autor*innen der Med Uni Graz
- Spener Friedrich
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- Abstract:
- When a 100,000 X g supernatant from bovine heart was incubated with [1-14C]oleic acid and subjected to isoelectric focusing, two fatty acid binding proteins (FABPs) with isoelectric points at 4.9 and 5.1 were detected. The proteins were purified on a large scale first by heat and acid precipitation of a postmitochondrial supernatant, as well as fractionation with ammonium sulfate, then by alternate application of ion-exchange and gel chromatography. The procedure afforded around 60 mg pure proteins from 1.5 kg fresh heart muscle. Relative molecular masses of 15 300 +/- 1600 for both proteins were derived from sodium dodecyl sulfate/polyacrylamide gel electrophoresis, gel chromatography, sedimentation velocity as well as from amino acid analysis. Up to 50% of the proteins' secondary structures consisted of beta-sheet. N-termini of the peptide chains were blocked; the amino acid compositions of the two proteins were similar, but differed considerably from those of the two FABPs isolated from bovine liver [Haunerland et al. (1984) Hoppe Seyler's Z. Physiol. Chem. 365, 365-376]. Whereas hepatic FABPs changed their pI upon binding fatty acids, cardiac FABPs did not. Cardiac FABPs were immunologically identical, but did not cross-react with hepatic proteins. A reversible, concentration-dependent self-association reported for FABP from pig heart [Fournier et al. (1983) Biochemistry 22, 1863-1872] was not observed for FABP from bovine heart. Changes of concentration did not alter secondary structure, intrinsic fluorescence or the sedimentation coefficient of the protein.
- Find related publications in this database (using NLM MeSH Indexing)
- Amino Acids - analysis
- Animals -
- Carrier Proteins - isolation and purification
- Cattle -
- Circular Dichroism -
- Cytosol - analysis
- Electrophoresis, Polyacrylamide Gel -
- Fatty Acid-Binding Proteins -
- Immunochemistry -
- Isoelectric Focusing -
- Liver - analysis
- Molecular Weight -
- Myocardium - analysis
- Neoplasm Proteins -
- Organ Specificity -
- Spectrometry, Fluorescence -
- Ultracentrifugation -