The protein moiety of endotoxin from Yersinia pseudotuberculosis: general characterization

T. F. Solov'eva, S.I. Bakholdina, I. M. Yermak, V. A. Khomenko, L. I. Fedoreyeva, O. D. Novikova, G. M. Frolova, G. N. Likhatskaya, Yu. S. Ovodov

Pacific Institute of Bioorganic Chemistry, Far East Division, Academy of Sciences of

the USSR, Vladivostok

Abstract: The protein moiety of endotoxin from Yersinia pseudotuberculosis was found to consist of two polypeptides with apparent molecular masses 40 and 14,5 kDa (4:1 w/w). The major protein (40 kDa) was isolated from the endotoxin pretreated with sodium deoxycholate by gel chromatography on the Sephadex G-200 column. Comparative study of this protein and oligomeric form of porin from the outer membrane of Y. pseudotuberculosis using SDS PAGE, velocity sedimentation, lipid bilayer experiments, chemical and serological analyses revealed their identity. The deoxycholate treatment of the endotoxin does not affect complexes of the major protein and LPS.

Russian Journal of Bioorganic Chemistry 1990, 16 (10):1301-1309

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