Kaidow A, Kataoka T, Wachi M, Takada A, Yamasaki M, Nagai K
Department of Bioengineering, Tokyo Institute of Technology, Kanagawa, Japan.
J Bacteriol. 1992 Aug;174(16):5454-6. doi: 10.1128/jb.174.16.5454-5456.1992.
Three proteins with molecular masses of 35, 55, and 75 kDa were found in an oriC complex fraction after purification through CsCl density gradient centrifugation (W. G. Hendrickson, T. Kusano, H. Yamaki, R. Balakrishnan, M. King, J. Murchie, and M. Schaechter, Cell 30:915-923, 1982). Of these three proteins, the 55-kDa protein was determined to be glycogen synthase on the basis of the N-terminal amino acid sequence and the molecular weight. The oriC complex was formed in glgA mutant cells, which produce no detectable glycogen, as well as in wild-type cells. None of the 35-, 55-, and 75-kDa proteins were detected in the fraction from this mutant. The results indicate that these proteins were not constituents of the oriC complex.
通过氯化铯密度梯度离心纯化后,在oriC复合组分中发现了分子量分别为35、55和75 kDa的三种蛋白质(W.G.亨德里克森、T.草野、H.山木、R.巴拉吉什南、M.金、J.默奇和M.沙赫特,《细胞》30:915 - 923,1982年)。在这三种蛋白质中,根据N端氨基酸序列和分子量确定55 kDa的蛋白质为糖原合酶。oriC复合物在不产生可检测糖原的glgA突变细胞以及野生型细胞中形成。在该突变体的组分中未检测到35 kDa、55 kDa和75 kDa的蛋白质。结果表明这些蛋白质不是oriC复合物的组成成分。