Abstract
The dissociation of the protein-peptidoglycan (PPG) complex from the outer membrane ofYersinia pseudotuberculosis has given two protein fractions consisting predominantly of two polypeptides. A decrease in the electrophoretic mobility of the high-molecular-weight polypeptide on treatment with detergent and on heating is connected with conformational transitions: β form → α-helix. The polypeptides were obtained in the individual state by gel filtration on Bio-Gel. They are immunogenic for rabbits and exhibit antigenic relationship in the double immunodiffusion reaction in agar.
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Pacific Ocean Institute of Bioorganic Chemistry, Far Eastern Scientific Center, Academy of Sciences of the USSR, Vladivostok. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 359–366, May–June, 1983.
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Novikova, O.D., Nabiullin, A.A., Solov'eva, T.F. et al. Isolation and characteristics of the proteins of the outer membrane of Yersinia pseudotuberculosis. Chem Nat Compd 19, 339–345 (1983). https://doi.org/10.1007/BF00579772
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DOI: https://doi.org/10.1007/BF00579772