Hitotsubashi S, Fujii Y, Okamoto K
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Japan.
FEMS Microbiol Lett. 1994 Oct 1;122(3):297-302. doi: 10.1111/j.1574-6968.1994.tb07183.x.
The protein binding Escherichia coli heat-stable enterotoxin II (STII) was isolated from cell membranes of mouse intestine. The binding of 125I-labeled STII to the proteins was inhibited by unlabeled STII, showing that it is specific. Proteins cross-linked with 125I-STII were purified by column chromatography on hydroxyapatite and TSK gel. Analyses of the purified protein by SDS-polyacrylamide gel electrophoresis and gel filtration showed that the molecular mass was 25 kDa.
从小鼠肠道细胞膜中分离出与蛋白质结合的大肠杆菌热稳定肠毒素II（STII）。未标记的STII可抑制125I标记的STII与蛋白质的结合，表明这种结合具有特异性。通过羟基磷灰石和TSK凝胶柱色谱法纯化与125I-STII交联的蛋白质。对纯化后的蛋白质进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和凝胶过滤分析，结果显示其分子量为25 kDa。
