Creeger E S, Chen J F, Rothfield L I
J Biol Chem. 1979 Feb 10;254(3):811-5.
A hybrid ColE1 plasmid containing DNA from Escherichia coli K12 were identified which was capable of correcting the defect in UDP-galactose:lipopolysaccharide alpha1,3-galactosyltransferase in an rfaH mutant of Salmonella typhimurium. Expression of the gene for this enzyme was also demonstrated in several strains of E. coli by direct assay. The E. coli and S. typhimurium enzymes are similar in catalytic properties and immunologic specificity. The finding of the galactosyltransferase activity in E. coli extracts is surprising since the alpha1,3-galactosylglucose disaccharide which is the product of the enzyme-catalyzed reaction does not appear to be present in the E. coli lipopolysaccharide.
已鉴定出一种含有来自大肠杆菌K12 DNA的杂种ColE1质粒，它能够校正鼠伤寒沙门氏菌rfaH突变体中UDP-半乳糖：脂多糖α1,3-半乳糖基转移酶的缺陷。通过直接测定法还证明了该酶基因在几种大肠杆菌菌株中的表达。大肠杆菌和鼠伤寒沙门氏菌的酶在催化特性和免疫特异性方面相似。在大肠杆菌提取物中发现半乳糖基转移酶活性令人惊讶，因为酶催化反应的产物α1,3-半乳糖基葡萄糖二糖似乎不存在于大肠杆菌脂多糖中。
