大鼠中的酰基辅酶A结合蛋白。纯化、结合特性、组织浓度及氨基酸序列。
Acyl-CoA-binding protein in the rat. Purification, binding characteristics, tissue concentrations and amino acid sequence.
作者信息
Knudsen J, Højrup P, Hansen H O, Hansen H F, Roepstorff P
机构信息
Institute of Biochemistry, Odense University, Denmark.
出版信息
Biochem J. 1989 Sep 1;262(2):513-9. doi: 10.1042/bj2620513.
Abstract
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.
摘要
酰基辅酶A结合蛋白（ACBP）是从大鼠肝脏中纯化得到的。通过质谱法测定其相对分子质量为9932±10，根据序列计算得出为9937.8。该蛋白能以高亲和力结合酰基辅酶A酯（C8 - C16），但无法结合脂肪酸。ACBP主要（86%）存在于可溶性组分中，在肝脏中的浓度最高，为5 - 6微克/毫克可溶性蛋白。通过气相埃德曼降解法和质谱法相结合确定了其完整的一级结构。大量使用252Cf等离子体解吸质谱法有助于肽段的鉴定和验证。与先前测定的牛酰基辅酶A结合蛋白序列进行比较，发现序列相似度非常高（83%），所有差异都可归因于单碱基变化。
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