PROTEIN HOMOLOGOUS TO THE GROEL GENE TRANSLATION PRODUCT OF ESCHERICHIA-COLI - ISOLATION AND PURIFICATION FROM THE MEMBRANE-FRACTION OF THEMARINE ALKALOTOLERANT BACTERIUM VIBRIO-ALGINOLYTICUS

Polypeptide with a molecular mass of aproximately 60 kDa was purified from the membrane fraction of the marine alkalotolerant bacterium Vibr io alginolyticus. Comparison of N-amino acid sequences of the 60-kDa p rotein and the gro EL translation product of E. coli and the molecular masses of the monomeric and oligomeric forms of these protein suggest ed these two proteins to be homologous to each other. Studies of the s olubilization of 60-kDa protein from the membrane under different cond itions by means of the immunoblotting technique with polyclonal antibo dies revealed loose association of this protein with the membrane frac tion of the V. alginolyticus.