Electron Microscopy Study of Anterior Neuropituitary of the Sterlet Acipenser ruthenus

Structural organization of sterlet anterior neuropituitary (ANP), a homologue of the median tubercle of Tetrapoda, was studied by method of electron microscopy. The ANP was conventionally divided in three zones in dorsoventral direction. Neurosecretory fibers (NsF) were concentrated mainly in the central and in the external zones. Terminals of NsF are directly adjacent to the basal membrane (BM) of the brain vascular sheath to form a morphological substrate for release of neurohormones into the pericapillary space. The presence of invaginations of the brain connective tissue sheath, which are in a close contact with NsF, indicates an increase of the area of neurosecretory contacts. Neurosecretory granules (NsG) of various shape and size are revealed in NsF and their terminals. Comparison of light-microscopy immunohistochemical data with localization of NsF terminals containing NsG of different diameters allows reconstructing distribution of neurosecretory elements of various ergicity in the ANP. Patterns of co-localization of various biologically active substances were revealed in the same varicose dilatations or terminals. Detection of typical synaptic contacts in the sterlet ANP indicates possibility of the cholinergic pituitary regulation, alongside with the peptide- and monoaminergic regulation.     

Growth and luminescence of luminous bacteria promoted by agents of microbial origin

The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleosides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, ironoxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.     

Isolation and properties of carboxylesterase from hemolymph of the silkworm Bombyx mori L

An original procedure for isolation and purification of carboxylesterase from the hemolymph of stage V larvae of one of Bombyx mori strains including precipitation with 10% polyethyleneglycol, ion-exchange chromatography on Sephadex G-200 and chromatography on DEAE-Sephadex A-50, has been developed. The specific activity of the enzyme after purification makes up to 1250 units per mg of protein with a 59% yield. Some physicochemical properties of the enzyme (Mr = 69 000, pI congruent to 4.9, temperature optimum = 40 degrees, pH optimum = 7.2 Km for alpha-naphthyl- and beta-naphthylacetate = 0.11 X 10(-3) and 0.52 X 10(-3) M, respectively) have been determined. Using immunodiffusion in agar gel, the antigenic identity of the enzymes isolated from the hemolymph of two silkworm species has been established.