[Stimulation of regenerative processes and correction of the functional activity of the liver in its partial resection and toxic lesions].

The effects of hepatotropic growth factors (HGFs) and phospholipid drugs on the recovery of functions and the regeneration of the rat liver were studied in CC14-induced toxic damage and after partial hepatectomy (PHE). HGFs isolated from the cytoplasmic cells of the regenerating liver, as well as from the liver of the animals given prodigiozan and from the media taken after culturing the explants of the regenerating liver were found to stimulate DNA synthesis and hepatocytic proliferation following PHE and in the cirrhotic liver. Prodigiozan was shown to induce the formation of HGFs not only in the rat liver following PHE, but in the liver of intact animals.

[The effect of covalently and noncovalently bound complexes of albumin with bilirubin on DNA and protein synthesis in liver and spleen of rats subjected to splenectomy and partial hepatectomy].

Noncovalently bound complexes of albumin and bilirubin were found to stimulate DNA and protein synthesis in partially hepatectomized regenerating rat liver tissue, while the covalently bound complex inhibited both these synthesis types in liver tissue after partial hepatectomy. Splenectomy of intact rats caused an induction of DNA and protein synthesis in liver tissue but partial hepatectomy decreased drastically the synthesis rate in spleen, thus suggesting that humoral factors stimulating the proliferation response in liver and spleen tissues were developed after spleen- and hepatectomies. The covalently bound albumin and bilirubin complex did not affect the rate of DNA and protein synthesis in liver tissue of splenectomized rats, while the complex with noncovalent bonds restored the rate of DNA and protein synthesis in the spleen of rats with partial hepatectomy.

Use of biospecific interactions of collagen, fibronectin and their fragments in affinity chromatography.

Various aspects of the application of fibronectin-collagen biospecific interactions in affinity chromatography are described. A new biospecific method for one-stage isolation of collagen peptides containing fibronectin-binding sites is proposed. The alpha 1 CB7-peptide of type-I collagen cyanogen bromide cleavage was isolated by means of affinity chromatography on adsorbents containing an immobilized gelatin-binding domain (45,000 relative molecular mass) of fibronectin.

[Isolation and purification of biopolymers using an affinity chromatography method. IX. Preparation, properties and use of affinity adsorbents with immobilized polypeptide fragments of collagen].

Synthesis and properties of new affinity adsorbents with immobilized polypeptide fragments of collagen molecule (alpha-chains, beta-components, cyanogen bromide peptides) were described. Adsorbents with alpha-chains and alpha 1CB7-peptide had fibronectin binding capacity 1.5-2.