Monitoring of Phytoplankton and Hydrochemical Parameters of Coastal Waters of Russky Island (Peter the Great Bay,Sea of Japan)

Russian Journal of Marine Biology - This paper presents the results of the study of the species composition and seasonal dynamics of the qualitative characteristics of phytoplankton in Paris and...     

cAMP-binding protein--a protein kinase of the plague pathogen]

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.     

The mediator mechanisms of the ventral hippocampus in anxiety states formed by different aversive exposures]

Microinjections of monoamines and amino acids into rat ventral hippocampus showed functional relevance of GABA- or dopamine- and 5-HT-ergic mechanisms of this structure of brain formed by aversive actions of diverse biological importance rather than glutamate-ergic ones. The participation of hippocampus monoamine- and acidergic mechanisms in the origin of diverse aversive anxiety is discussed.     

Separation of racemic <Emphasis Type="Italic">ortho</Emphasis>-isobornylphenol into enantiomers and evaluation of their antioxidant activity

Racemic ortho-isobornylphenol was separated into enantiomers through diastereomeric camphanates. The absolute configuration of chiral centers of the isolated products was determined by X-ray studies. Antioxidant activity and membrane-protective properties of the enantiomers were studied on the model of H₂O₂-induced hemolysis of erythrocytes.