Jensen M S, Højrup P, Rasmussen J T, Knudsen J
Institute of Biochemistry, Odense University, Denmark.
Biochem J. 1992 Jun 15;284 ( Pt 3)(Pt 3):809-12. doi: 10.1042/bj2840809.
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 ACBP 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 Lys18 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.
在从牛肝脏中纯化得到的酰基辅酶A结合蛋白（ACBP）中鉴定出四种不同修饰形式。在等电聚焦中，大部分纯化的ACBP聚焦在pH 5.9，并且可以证明是未经任何进一步修饰的N - 乙酰化ACBP。两个较小的峰分别聚焦在pH 5.25和4.85。质谱分析和序列测定表明，pI 5.25的形式在赖氨酸18处被乙酰化，而pI 4.85的形式在同一位置被丙二酰化。此外，还可以证明在纯化过程中发生了非酶糖基化。ACBP的乙酰化和丙二酰化变体仅在成年牛中发现。
