Staun M, Sjöström H, Norén O
Eur J Clin Invest. 1986 Dec;16(6):468-72. doi: 10.1111/j.1365-2362.1986.tb02163.x.
A calcium-binding protein (CaBP) was purified from human small intestinal mucosa by ammonium sulphate fractionation, gel filtration and chromatofocusing. Antibodies against CaBP were raised in rabbits and CaBP was then isolated from human intestinal cytosol by a one-step immunoadsorbent procedure. In polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate CaBP migrated as a single band corresponding to a molecular weight of 10,000. The calcium-binding ability of CaBP was demonstrated by increased electrophoretic mobility of CaBP in the presence of EDTA as demonstrated by immunoblotting of agarose gels. CaBP antibody showed no cross reaction with cytosolic proteins of duodenum from rat or pig. The present study suggests that molecular properties and distribution of human intestinal CaBP is comparable to those of intestinal CaBP detected in lower mammalian species.
通过硫酸铵分级分离、凝胶过滤和色谱聚焦从人小肠黏膜中纯化出一种钙结合蛋白（CaBP）。用兔制备了抗CaBP抗体，然后通过一步免疫吸附程序从人肠细胞溶质中分离出CaBP。在十二烷基硫酸钠存在下的聚丙烯酰胺凝胶电泳中，CaBP迁移为一条单一的条带，对应分子量为10,000。通过琼脂糖凝胶免疫印迹证明，在EDTA存在下CaBP的电泳迁移率增加，从而证明了CaBP的钙结合能力。CaBP抗体与大鼠或猪十二指肠的细胞溶质蛋白无交叉反应。本研究表明，人肠CaBP的分子特性和分布与在低等哺乳动物中检测到的肠CaBP相当。
