[A cyclic 3',5'-adenosine monophosphate-binding protein in the causative agent of plague].

cAMP-binding protein was isolated from the plaque agent and purified to the homogeneous state. Purification process included filtration of the initial preparation through the membrane able to transmit particles with mol. weight to 300,000 Da, chromatography on cellulose "DE-52" and biogel HTP. The protein homogeneity was confirmed by electrophoresis in polyacrylamide gel and precipitation with commercial plague agglutinating serum. The protein with mol. weight of 180,000 Da consisted of two identical subunits (90,000 Da. each) which could dissociate with formation of monomers (mol. weight approximately 18,000 Da), Cu2+, Co2+, Mn2+ ions stimulated activity of cAMP-binding protein of a plague microbe while Fe3+, Ca2+, Zn2+ ions inhibited it by 30-70%. A monospecific rabbit serum to the homogeneous preparation of cAMP-binding protein was obtained. It helped finding the similar protein in the close relative bacterium Yersinia pseudotuberculosis but not in Y. enterocolitica.