[Biologically Active Peptides of King Crab Hepatopancreas].

Substances of a peptide nature isolated from the hepatopancreas of the king crab Paralithodes camtschaticus exhibited physicochemical properties and membranotropic and specific activities similar to those of membranotropic homeostatic tissue-specific bioregulators previously found in different mammalian and plant tissues. Their biological effect on vertebrate tissues was demonstrated on a model of roller organotypic cultivation of Pleurodeles waltl newt liver tissue.

[Peptide-containing fraction from a culture medium of Fusarium sambucinum: composition and biological effects].

The culture fluid of the fungus Fusarium sambucinum was investigated for the presence of new peptide-containing bioregulators, previously identified in various mammalian and plant tissues. A fraction containing peptides with molecular weights from 1000 to 2000 Da, which exhibited specific membranotropic activity and a number of physical and chemical properties characteristic of this group of bioregulators, was obtained. The effects of this fraction on the model roller organotypic cultivation of liver tissue of the Pleurodeles waltl newt in vitro were investigated for the first time. This fraction caused the additional activation of pigmented liver cells of newt (analogues to Kupffer cells of the liver of mammals) and provided the maintenance of cell-cell adhesive interactions in tissues. The results show that a new group of peptide bioregulators was present in the culture medium of the fungus F. sambucinum.

Analysis of a bioregulator isolated from rat testes in roller organotypic culture of mouse testes in vitro.

A new bioregulator, a representative of membranotropic homeostatic tissue-specific bioregulators acting in ultralow doses, was isolated from rat testes. A model of roller organotypic culturing of mouse testes was developed and the protective effect of the bioregulator was analyzed.

Structural-functional characteristics of a new bioregulator isolated from bovine pigmented epithelium tissue.

A new bioregulator operating in ultralow doses corresponding to 10(-17) mg/ml has been isolated from tissue of pigmented epithelium of bovine eyes. It has been established that the functional basis of this bioregulator is a complex of a low molecular weight regulatory peptide (4372 Da) and a modulator consisting of a mixture of proteins with molecular weights of 14.980-66.283 kDa. It has been shown that the regulatory peptide is responsible for membranotropic activity of the bioregulator, and the modulator proteins are responsible for biological action in ultralow doses. The data demonstrate an interrelation between nanocondition of the bioregulator and its ability to show activity in ultralow doses.

[Modulators of the regulatory protein activity acting at microdoses].

New, previously not studied bioregulators active in the ultra low doses corresponding of 10(-8) - 10(-17) mg/ml have been isolated from vitreoretinal tissue of eye. It has been shown that these bioregulators comprise some regulatory peptides-modulators represented by proteins with molecular weights 15-70 KDa one of which is bovine serum albumin. Correlation between the nanosize of bioregulators and their ability to show activity in ultra low doses is established.

[New liposomal forms of antifungal antibiotics, modified by amphiphilic polymers].

A method has been developed, for incorporating macrocyclic polyene antibiotics nistatin and amphotericin B into liposomes containing phosphatidylcholine and cholesterol (7:3) or phosphatidylcholine, cholesterol, and cardiolipin (7:3:1), the membranes of which were modified with an amphiphilic polymer of N-vinylpyrrolidone, carrying one terminal n-octadecyl group and having a molecular weight of 4000 Da. The amount of antibiotics within such liposomal nanocarriers may be as high as 17-22%. It was demonstrated that the modified liposomes have sizes in the range 150-200 nm and exhibit increased long-term storage stability and increased resistance to disrupting agents (Triton X-100 or ethanol) and ultrasound. The antifungal activity of the liposomal preparations obtained exceeded that of the antibiotics not subjected to immobilization.

[Primary structure of a short toxin from the venom of a vietnamese scorpion (Buthus sp.)]. / Pervichnaia struktura korotkogo toksina iz iada v'etnamskogo skorpiona Buthus sp.

The complete amino acid sequence of an important toxin (toxin 14) from the venom of a Vietnamese scorpion (Buthus occitanus sp.) has been determined, which includes 35 amino acid residues and three disulfide bridges (molecular weight, 3843 Da). The comparison of the sequence with sequences of short scorpion toxins led us to conclude that toxin 14 belongs to a novel group of toxins affecting the excitability of myelinated nerves.

[Isolation and some properties of a lectin from the venom of the Vietnamese scorpion Buthus occitanus sp]. / Vydelenie i nekotorye svoistva lektina iz iada V'etnamskogo skorpiona Buthus occitanus sp.

A lectin was isolated from the venom of scorpion Buthus occitanus sp. by means of Sephadex G-50 gel filtration and CM-cellulose ion exchange chromatography. The homogeneous lectin preparation consisted of homodimeric molecules with a subunit Mr of 9.3 kDa. Glycine, alanine, and serine dominated in the lectin amino acid composition. The lectin was a glycoprotein containing 20% carbohydrates (predominantly mannose and glucose). Trypsin-treated murine erythrocytes agglutinated at the lectin concentration of 32 micrograms/ml. Hemagglutination was inhibited by carbohydrates (L-fucose > D-glucose > L-rhamnose > D-xylose). The lectin revealed no phospholipase or hyaluronidase, nor toxic activity.

Isolation of toxins from Buthus occitanus sp. scorpion and their action on excitability of myelinated nerve.

A series of short neurotoxins (molecular weight 3500-5000 D) was isolated from Vietnamese scorpion B. occitanus sp. All these toxins blocked generation of action potentials (this effect depended on their molecular weight), but did not change conduction velocity and excitation threshold of the nerve.

[Isolation and characteristics of a lectin-like protein from bee venom]. / Vydelenie i kharakteristika lektinopodobnogo belka iz pchelinogo iada.

Lectin-like properties of bee venom proteins were studied. Phospholipase A2 was demonstrated to harbor lectin activity. Specific hemagglutinating activity of the isolated phospholipase exceeded 320 times the activity of the initial bee venom.