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

J. Knudsen, P. Hojrup, H. O. Hansen, H. F. Hansen, P. Roepstorff

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Abstrakt

Acyl-CoA-binding protein (ACBP) was purified from rat liver. The M(r) 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 μg/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.

OriginalsprogEngelsk
TidsskriftBiochemical Journal
Vol/bind262
Udgave nummer2
Sider (fra-til)513-519
Antal sider7
ISSN0264-6021
DOI
StatusUdgivet - 1. jan. 1989

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