Identical reactivity of brain and erythrocyte cholinesterases of some mammals

The paper deals with a comparative study of various aspects of reactivity (substrate and inhibitor specificity, sensitivity to action of hydrophobic organophosphorus inhibitors, capability for reactivation) of cholinesterase preparations from brain, erythrocytes, and serum of a group of mammals (human, rabbit, rat, cattle, dog, and cat). It has turned out that at preservation of the species and tissue specificity, catalytic properties of the brain and erythrocyte cholinesterases of the same animal species are very close to each other.     

Comparative-enzymologic study of phosphatase activity of Pacific hydrobionts

Activities of acid phosphatase are studied with use as substrates of phenyl phosphate, α- and β-glycerophosphates in various organs and tissues of a large group of marketable hydrobionts of the Pacific basin (12 fish species, 7 invertebrate species, and one mammalian species) and of alkaline phosphatase in various organs of the Commander (Berryteuthis magister) and the New Zealand (Nototodarus sloani sloani) squids. Intertissue and interspecies differences have been revealed in the substrate and inhibitory specificity of the studied enzyme preparations. The method of isolation and a partial purification of preparations of acid phosphatase from tissue of gonads and of alkaline phosphatase from tissues of kidney and liver of individuals of marketable squid species are described.