Timanova A M, Marti T, Walter R D, Bankov I Y
Institute of Experimental Pathology and Parasitology, Bulgarian Academy of Sciences, Sofia.
Parasitol Res. 1997;83(5):518-21. doi: 10.1007/s004360050291.
A 12-kDa fatty-acid-binding protein was purified to homogeneity from Ascaris suum reproductive tissue as confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. N-terminal amino-acid-sequence analysis of the protein revealed its identity with the ABA-1 allergen protein isolated from A. suum pseudocoelomic fluid. Fatty-acid binding by the protein from A. suum reproductive tissue was investigated using the Lipidex 1000 assay, which revealed the presence of a single class of fatty-acid-binding sites with an apparent dissociation constant for palmitate of about 0.8 microM.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳证实，从猪蛔虫生殖组织中纯化出一种12千道尔顿的脂肪酸结合蛋白，达到了同质纯。对该蛋白进行N端氨基酸序列分析，结果显示它与从猪蛔虫假体腔液中分离出的ABA-1变应原蛋白相同。使用Lipidex 1000分析法研究了猪蛔虫生殖组织蛋白的脂肪酸结合情况，结果表明存在一类单一的脂肪酸结合位点，棕榈酸的表观解离常数约为0.8微摩尔。
