Abstract
Lipopolysaccharides, extracted by phenol/chloroform/petroleum ether, from two rough mutants of Salmonella typhimurium of class rfaH were studied by passive haemagglutination inhibition and by methylation analysis. The structural and immunochemical analyses showed that (i) formation of the galactose I unit of the core is defective, but the defect is not complete, and (ii) of those core chains which do receive the galactose I residue, many are not continued to form complete core, but instead terminate at intermediate points. This suggests that the rfaH gene, though involved in formation of the galactose I unit, is not the structural gene for the galactosyltransferase which adds this unit. The rfaH product may be a positive regulator for several rfa genes specifying glycosyltransferases, or it may be a protein needed for the efficient action of several such transferases.
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