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Titlebook: Cellular Fatty Acid-binding Proteins; Jan F. C. Glatz,Ger J. Vusse Book 1990 Springer Science+Business Media Dordrecht 1990 heart.membrane

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13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty acid-binding proidual binding sites on proteins has been developed. The utility of this method results from the high degree of resolution of carboxyl from other carbon resonances and the high sensitivity of FA carboxyl chemical shifts to intermolecular environmental factors such as degree of hydrogen-bonding or hyd
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Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gelsose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABP. with M. 15 kDa has been purified from human heart muscle and found to be present in levels 2–4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel e
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Role of fatty acid-binding protein in cardiac fatty acid oxidation,a function. Because of its strong affinity for long chain fatty acids and its cytoplasmic origin, this protein was repeatedly claimed in the literature to be the transcytoplas-mic fatty acid carrier. However, techniques to visualize and quantify the movements of molecules in the cytoplasm are still
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https://doi.org/10.1007/978-3-531-19237-6d to the function of the cells in liver, muscle and kidney. The presence of FABP in cellular organelles requires more evidence. The functional significance of the occurrence of more FABP types is unclear, in spite of the observed differences in their ligand-protein interaction.
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,The case for “Local Oil Nationalism”,for palmitic acid. The complete amino acid sequence of the brain FABP was determined and a microheterogeneity was observed. Sequence comparison with other FABPs of known sequence and the observed microheterogeneity demonstrated the presence in brain of several homologous FABPs closely related to heart FABP.
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