title: [cAMP-binding protein--a protein kinase of the plague pathogen].
abstract: In Y. pestis a cyclic AMP-binding protein was detected, isolated to a homogeneous state, and its physico-chemical properties were studied. The protein is a highly molecular compound with a molecular weight of 180 kD, capable of being released into the environment in the process of cell growth and having protein kinase activity, not depending on the presence of cyclic AMP. Y. pestis neuraminidase is one of the substrates appearing due to the action of protein kinase detected in this study. Y. pestis protein kinase may alter the spectrum of protein phosphorylation in the leukocytes of white mice. The direct participation of this protein in the development of infection is supposed.
authors.forename: L A
authors.initials: LA
authors.lastname: Shevchenko
authors.forename: N Ia
authors.initials: NIa
authors.lastname: Shimaniuk
authors.forename: B N
authors.initials: BN
authors.lastname: Mishan'kin
mesh_terms: D001345:Autoradiography; D000242:Cyclic AMP / Q000378:metabolism*; D009439:Neuraminidase / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D015010:Yersinia pestis / Q000201:enzymology*
chemical_list: D000242:Cyclic AMP; D011494:Protein Kinases; D009439:Neuraminidase
vernacular_title: TsAMF-sviazyvaiushchiĭ belok--proteinkinaza vozbuditelia chumy.