Acyl-CoA-binding protein in the rat. Purification, binding characteristics, tissue concentrations and amino acid sequence

• Published in: Biochemical journal Vol. 262; no. 2; pp. 513 - 519
• Main Authors: Knudsen, J, Højrup, P, Hansen, H O, Hansen, H F, Roepstorff, P
• Format: Journal Article
• Language: English
• Published: England 01.09.1989
• Subjects: Acyl Coenzyme A - metabolism; Amino Acid Sequence; Animals; Carrier Proteins - analysis; Carrier Proteins - isolation & purification; Carrier Proteins - metabolism; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty Acids - metabolism; Liver - analysis; Molecular Sequence Data; Neoplasm Proteins; Nerve Tissue Proteins; Rats
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2620513

Acyl-CoA-binding protein (ACBP) was purified from rat liver. The Mr was determined as 9932 +/- 10 by mass spectrometry and calculated as 9937.8 from the sequence. The protein binds acyl-CoA esters (C8-C16) with high affinity, but was unable to bind fatty acids. ACBP was found mainly (86%) in the soluble fraction, and the concentration was highest in liver, 5-6 micrograms/mg of soluble protein. The complete primary structure was determined by a combination of gas-phase Edman degradations and mass spectrometry. Extensive use of 252Cf plasma-desorption mass spectrometry facilitated the identification and verification of peptides. Comparison with the previously determined sequence of bovine acyl-CoA-binding protein revealed a very strong sequence similarity (83%), and all of the differences could be accounted for by single base changes.