来自人类骨骼肌的脂肪酸结合蛋白。

The fatty acid-binding protein from human skeletal muscle.

作者信息

Peeters R A, in't Groen M A, Veerkamp J H

机构信息

Department of Biochemistry, University of Nijmegen, The Netherlands.

出版信息

Arch Biochem Biophys. 1989 Nov 1;274(2):556-63. doi: 10.1016/0003-9861(89)90470-0.

DOI:10.1016/0003-9861(89)90470-0

PMID:2802628

Abstract

Fatty acid-binding protein (FABP) was isolated from human skeletal muscle by gel filtration and anion- and cation-exchange chromatography. The isolation procedure, however, with rat and pig skeletal muscle gave mostly inactive preparations. Rat muscle FABP preparations contained parvalbumin as a contaminant. FABP from human muscle had a Mr of about 15 kDa, a pI value of 5.2, and a Kd value with oleic acid of 0.50 microM. Skeletal muscle and heart FABPs and their antisera showed a strong cross-reactivity on Western blots and in enzyme-linked immunosorbent assays (ELISA). No cross-reactivity was observed with liver FABP and its antiserum. On the basis of amino acid composition, electrophoretic behavior, fatty acid binding, and immunochemical properties, human skeletal muscle FABP must be similar or closely related to human heart FABP. The FABP content determined by ELISA was comparable in various human muscles and cultured muscle cells, but lower than that in rat muscles.

摘要

通过凝胶过滤以及阴离子和阳离子交换色谱法从人骨骼肌中分离出脂肪酸结合蛋白（FABP）。然而，用大鼠和猪的骨骼肌进行分离时，大多得到无活性的制剂。大鼠肌肉FABP制剂含有副肌球蛋白作为污染物。人肌肉中的FABP的相对分子质量约为15 kDa，等电点值为5.2，与油酸的解离常数（Kd）值为0.50 μM。骨骼肌和心脏FABP及其抗血清在蛋白质印迹法和酶联免疫吸附测定（ELISA）中显示出强烈的交叉反应性。未观察到与肝脏FABP及其抗血清有交叉反应性。基于氨基酸组成、电泳行为、脂肪酸结合和免疫化学特性，人骨骼肌FABP必定与人心脏FABP相似或密切相关。通过ELISA测定的FABP含量在各种人肌肉和培养的肌肉细胞中相当，但低于大鼠肌肉中的含量。