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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Detection, tissue distribution and (sub)cellular localization of fatty acid-binding protein types,on and their binding properties. Besides the 3 well-known liver, heart and intestinal types, new types as the adipose tissue, myelin and (rat) renal FABPs have been described. Recent observations suggest the occurrence of more tissue-specific types, e.g. in placenta and adrenals. Heart FABP is widel

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Fatty acid oxidation capacity and fatty acid-binding protein content of different cell types isolat from the cellular membrane to the intracellular site of oxidation and also, in case of endothelial cells, in the transfer of fatty acids from the vascular to the interstitial compartment through the endothelial cytoplasm. The present study was designed to delineate a possible quantitative relations

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Localization of liver fatty acid-binding protein and its mRNA in the liver and jejunum of rats: an ans of immunohistochemistry using a specific antibody to L-FABP and . hybridization using a synthetic oligonucleotide complementary to L-FABP mRNA as probe. In the liver from normally fed rats, the signal for L-FABP mRNA in hepatocytes was distributed throughout the lobule, with higher intensity in

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Type-specific immunodetection of human heart fatty acid-binding protein with polyclonal anti-peptid each and corresponding with different antigenic parts of the human H-FABP. molecule, were synthesized. Polyclonal antibodies against these synthetic peptides were raised in mice (Balb/C) and rabbits (Flemish giant). When tested in enzyme linked immunosorbent assays (ELISA, antibody-capture assay),

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Characteristics of fatty acid-binding proteins and their relation to mammary-derived growth inhibit, namely the hepatic-, intestinal- and cardiac-type. Highly conserved sequences of FABPs within the same type correlate with immunological crossreactivities. Isoforms of hepatic-type FABP are found in several mammalian species and for bovine liver FABP specific shifts in isoelectric points upon lipi

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Expression of fatty acid-binding protein from bovine heart in ,,isopropyl-β-D-thiogalactopyranoside cFABP was found in a soluble form in the cytosol of plasmid transformed . amounting up to 5.7% of the soluble protein. cFABP was detected after SDS-polyacrylamide gelelectrophoresis and/or isoelectric focusing and Western blot by immuno-staining and was determined

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Expression of rat intestinal fatty acid binding protein in , and its subsequent structural analysis direct efficient synthesis of rat intestinal fatty acid binding protein (I-FABP) in .. Expression of I-FABP in . has no apparent, deleterious effects on the organism. High levels of expression of I-FABP mRNA in supE. strains of ., such as JM101, is associated with suppression of termination at its