Jomori T, Kubo T, Natori S
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Eur J Biochem. 1990 May 31;190(1):201-6. doi: 10.1111/j.1432-1033.1990.tb15565.x.
A protein having affinity to lipopolysaccharide of Escherichia coli K12 was purified to homogeneity from the hemolymph of Periplaneta americana. This protein, with an average molecular mass of 450 kDa. was a homooligomer of a 28-kDa subunit protein. Comparative studies using lipopolysaccharide molecules of E. coli and Salmonella minnesota suggested that this protein recognizes and binds to a specific carbohydrate structure of E. coli lipopolysaccharide. Ca2+ was required for this protein to bind to lipopolysaccharide, but other divalent cations could not replace Ca2+.
从美洲大蠊的血淋巴中纯化出一种对大肠杆菌K12脂多糖具有亲和力的蛋白质，且纯度达到了均一性。这种蛋白质的平均分子量为450 kDa，是由28 kDa亚基蛋白组成的同型寡聚体。使用大肠杆菌和明尼苏达沙门氏菌的脂多糖分子进行的比较研究表明，这种蛋白质能够识别并结合大肠杆菌脂多糖的特定碳水化合物结构。该蛋白质与脂多糖结合需要Ca2+，但其他二价阳离子无法替代Ca2+。
