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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Acyl-CoA-binding protein in the rat. Purification, binding characteristics, tissue concentrations and amino acid sequence. Knudsen, J., Højrup, P., Hansen, H.O., Hansen, H.F., Roepstorff, P. Biochem. J. (1989) [Pubmed]
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