Disease relevance of FABP1

• The coding part of the cDNA for bovine liver-type fatty acid binding protein (L-FABP) has been amplified by RT-PCR, cloned and used for the construction of an Escherichia coli (E. coli) expression system [1].

High impact information on FABP1

• When tryptic peptides of the pH 7.0/7.1 fraction were analyzed, discrepancies between sequence and mass data of the peptides containing at position 69 the sole cysteine of L-FABP led to the disclosure of a cysteinylation occurring at this position and giving rise to the slightly more basic pH 7.1 species [2].
• In none of the assays binding of cholesterol to L-FABP was observed [1].
• Dissociation constants for binding of oleic acid, arachidonic acid, oleoyl-CoA, lysophosphatidic acid and the peroxisomal proliferator bezafibrate to L-FABP have been determined by titration calorimetry [1].
• Furthermore, binding of cholesterol to L-FABP was investigated with the Lipidex assay, a liposome binding assay and a fluorescence displacement assay [1].

Associations of FABP1 with chemical compounds

• Together amino acid exchange and covalent modification of cysteine entirely explain the heterogeneity of L-FABP from bovine liver [2].

References