Whetstone H D, Hurley W L, Davis C L
Comp Biochem Physiol B. 1986;85(3):687-92. doi: 10.1016/0305-0491(86)90068-4.
A fatty acid binding protein (FABP) was isolated from bovine mammary cytosol by gel filtration and ion exchange chromatography. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate indicated a mol. wt. of 12,000. Isoelectric focusing showed two bands at pH 5.6 and 5.8. FABP bound long chain fatty acids and their CoA thioesters, but not medium or short chain fatty acids. Affinity constant (Ka) for 18:1 was about 2 micromolar. Endogenously bound fatty acids included 16:0, 18:0 and 18:1, in both covalent and noncovalent association with FABP. Activities of microsomal phosphatidic acid phosphatase, fatty acid:CoA ligase or diacylglycerol acyltransferase were not affected by purified FABP in vitro.
通过凝胶过滤和离子交换色谱法从牛乳腺细胞质中分离出一种脂肪酸结合蛋白（FABP）。十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示其分子量为12,000。等电聚焦在pH 5.6和5.8处显示出两条带。FABP结合长链脂肪酸及其辅酶A硫酯，但不结合中链或短链脂肪酸。18:1的亲和常数（Ka）约为2微摩尔。内源性结合的脂肪酸包括16:0、18:0和18:1，它们与FABP以共价和非共价方式结合。微粒体磷脂酸磷酸酶、脂肪酸：辅酶A连接酶或二酰基甘油酰基转移酶的活性在体外不受纯化的FABP影响。
