Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver

M. S. Jensen, P. Hojrup, J. T. Rasmussen, J. Knudsen*

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Abstrakt

Four differently modified forms of acyl-CoA-binding protein (ACBP) were identified in ACBP purified from bovine liver. The majority of the purified ACBP was focused at pH 5.9 in isoelectric focusing and could be shown to be N-acetylated AC 13P without any further modifications. Two minor peaks were focused at pH 5.25 and 4.85 respectively. Mass spectrometry and sequence determination showed that the pI 5.25 form was acetylated at Lys 18 and that the pI 4.85 form was malonylated in the same position. Furthermore, it could be shown that non-enzymic glycosylation occurred during purification. The acetylated and malonylated variants of ACBP were only found in adult cattle.

OriginalsprogEngelsk
TidsskriftBiochemical Journal
Vol/bind284
Udgave nummer3
Sider (fra-til)809-812
Antal sider4
ISSN0264-6021
DOI
StatusUdgivet - 1. jan. 1992

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