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T A Osipova

Publications and source records attributed to T A Osipova.

At least 19 recordsLinked to original sources
PubMed1997

[Hearing function of workers of "noisy" occupations at the Podolsk machinery plant and effectiveness of therapeutic measures].

In recent years noise and vibration have become dominant hazards influencing workers' health. A significant share of the resulting disease in covered by occupational deafness. The article demonstrates data of hearing examination among 262 workers exposed to intermittent noise of 95-100 dB A. Slow progress of occupational deafness and bilateral cochlear neuritis with over 15 years of service appeared to be characteristic for the examinees. Helium neon laser applied on mastoid process and general improving treatment appeared to be effective.

Adult↗
PubMed1992

[An electrophoretic analysis of human glycoprotein hormones and their subunits].

Stability of heterodimers of human glycoprotein hormones with gonadotropic and thyrotropic activities in sodium dodecylsulfate (SDS) under non-reducing conditions at low temperature permits to resolve the native molecules of these hormones in SDS-PAG and to distinguish from their dissociated subunits by electrophoretical mobility. The analysis of dimers and alpha-, beta-subunits in one polyacrylamide gel allows to detect certain human glycoprotein hormones and to study some of their physico-chemical properties. Using two polyclonal antisera against human LH and FSH by the Western blot immunoassay it was shown that heterodimers as well as alpha and beta subunits after SDS-PAGE retain antigenic activity of native hormones. The method gave possibility to characterize the specificity of the given sera to different glycoprotein hormones.

Animals↗
PubMed1989

[Obtaining of monoclonal antibodies to human growth hormone and their characteristics].

The aim of present study was to obtain the hybridomas producing monoclonal antibodies against human growth hormone (Mabs hGH), to investigate the properties of the obtained Mabs and the possibility of their application in immunoanalytical systems. Two hybridomas secreting Mabs against hGH and belonging to the IgGI subclass have been obtained. The cross-reactivity of the Mabs with structurally similar to hGH hormones (hGHbio, hPL, hPRL, bGH, bPRL, pPRL) using indirect IFA has been studied. It has been shown that Mabs hGHI and Mabs hGH2 are directed to common specific antigenic determinant i.e. they have the same epitope specificity and don't react with other structurally related hormones, i.-e. this determinant is unique for hGH. The obtained Mabs hGH2 would find application for determination hGH by immunochemical methods in fractions while the hormone isolation from pituitaries and hGH obtained recombinant DNA methodology. The development of immunosorbents on the basis Mabs hGH2 seems to be perspective. Application of this immunosorbent may give possibility to optimize hormone isolation process.

Animals↗
PubMed1984

[Induction of sensitivity of a fibroblast culture to hypophyseal somatotropin by a thermostable blood serum factor].

A study was made of the effects of highly purified preparations of human and bovine pituitary somatotropin on DNA biosynthesis in fibroblast cultures from adults' skin. The intensity of DNA biosynthesis was evaluated from 3H-thymidine incorporation into the cells. It was established that both somatotropin preparations are capable of stimulating DNA synthesis by fibroblasts. However, simultaneous presence in the medium of the thermo- and acid-resistant fractions of rat blood serum is required for the stimulating effect of the hormone to manifest. It was found that the activity of blood serum factor inducing fibroblast sensitivity to somatotropin depends on the pituitary and rises after hypophysectomy.

Adult↗
PubMed1983

The effect of synthetic fragment 31-44 of human growth hormone on glucose uptake by isolated adipose tissue.

Synthetic tetradecapeptide corresponding to amino acid sequence 31-44 of human growth hormone molecule and possessing a lipotropic activity was tested for the ability to stimulate glucose uptake by isolated epididymal fat pads of fed rats. Tetradecapeptide 31-44 (1 microgram/ml), growth hormone (1 microgram/ml) and insulin (50 microU/ml) stimulated in about equal degree the uptake of [U-14C]glucose by adipose tissue. Tissue samples were preliminary incubated for 3-4 hours in the absence of hormones to eliminate the refractoriness to the insulin-like effects of growth hormone. Without preincubation the tissue was refractory to the action of growth hormone and tetradecapeptide 31-44, but was sensitive to insulin. The data obtained together with the findings of Lewis et al., which showed that 20K structural variant of human growth hormone having the deletion of residues 32-46 cannot stimulate glucose uptake and lipolysis in rats, make it possible to suggest that both activities are associated with fragment 31-44.

Adipose Tissue↗
PubMed1983

[Not Available].

Explore the source record for details and available documents.

Biochemistry↗
PubMed1983

[New data on the biological activity of pituitary somatotropin fragment 77-107].

Some new evidence on the biological activity of somatotropin fragment 77-107 is given. This fragment was prepared from whale somatotropin by tryptic hydrolysis. Beside the previously established ability of the hormone to increase the width of the tibial epiphyseal cartilage in hypophysectomized rats ("tibia" test) two other properties of the fragment indicative of its growth-promoting activity were established. The fragment enhances DNA biosynthesis in cultured human fibroblasts and increases the somatomedin content in blood serum of hypophysectomized rats. However, the fragment unlike the native hormone does not exert any metabolic action on adipose tissue "in vitro", i. e. does not stimulate the nonesterified fatty acid release into the medium. A comparison of the biological activity spectrum of native somatotropin and of its fragment 77-107 suggests that the biochemical information required for the realization of a prolonged growth-promoting effect and a relatively rapid action of the hormone on lipid and carbohydrate metabolism is contained in different parts of the polypeptide chain.

Animals↗
PubMed1982

Primary structure of seiwhale pituitary somatotropin.

Seiwhale somatotropin has been isolated from seiwhale pituitaries. It was cleaved by cyanogen bromide, trypsin and chymotrypsin. The peptide fragments were separated and purified by gel filtration on Sephadexes, ion exchange chromatography, high voltage electrophoresis and paper chromatography. Amino acid sequences of the isolated peptides were studied by the dansyl-Edman procedure. The data obtained suggested a primary structure of seiwhale somatotropin consisting of 190 amino acid residues and showed a high degree of homology with somatotropins of many other species.

Amino Acid Sequence↗
PubMed1982

[Amino acid sequence of seiwhale somatotropin].

Thirteen homogenous peptides were isolated from the chymotryptic hydrolysate of seiwhale somatotropin. The amino acid composition and sequence of the chymotryptic peptides were determined. Two large peptides were isolated from the tryptic hydrolysate of the performic acid-oxidized somatotropin. One of them had 20 amino acid residues and contained cysteic acid; the other one consisted of 31 residues and contained tryptophane and numerous leucine residues. The amino acid sequence of tryptic peptides was established after their hydrolysis with chymotrypsin. Based on these and earlier published data a complete amino acid sequence of seiwhale somatotropin comprising 190 amino acid residues was proposed. O comparison of primary structure of somatotropins from 6 different sources revealed the most conservative and variable regions of the hormone polypeptide chain.

Amino Acid Sequence↗
PubMed1980

[Hydrophobic peptide possessing growth activity from the trypsin hydrolysate of sperm whale somatotropin].

Hydrophobic 31-member peptide exerting a considerable growth effect in "tibia-test" was extracted in a homogenous state from trypsin hydrolyzate of cachalot somatotropin. Comparison of N-end (1--11) aminoacid succession of peptide content with known somatotropin structure allows a conclusion that the peptide represents the 77th to 107th ingredient of the hormone polipeptide chain. The peptide studied has no analogues among somatotropin ingredients described in the literature capable of retaining the growth effect and having the shortest structure.

Amino Acid Sequence↗
PubMedDate not supplied

[Monoclonal antibodies to bovine prolactin interacting with human prolactin].

Two stable hybridomas producing antibodies (Mab 1 and Mab 2) to bovine prolactin and belonging to the IgG1 subclass have been prepared. The cross-reactivity of Mab 1 and Mab 2 with some structurally similar pituitary protein (human, pig, whale, rat prolactins, bovine and human somatotropins) using indirect immunoenzymatic assay, was studied. It has been shown that Mab 2 reacts specifically only with bovine prolactin whereas Mab 1 interacts with human prolactin and prolactins of different animals. The specificity of Mab 1 to human prolactin was confirmed by immunoradiodetection assay on nitrocellulose filters. The data obtained give evidence of the existence of at least two different sterically nonoverlapping epitopes: one of them is specific exclusively for bovine prolactin and the other one is common, i.e. extraspecific.

Animals↗
PubMedDate not supplied

[Hypoinsulinemia, hyperglycemia and circulating antibodies to the islet cells during the development of streptozotocin diabetes in rats].

The time course of metabolic parameters and islet cell surface antibodies (ICSA) in low-dose streptozotocin (STZ)-induced diabetes in rats was studied, a total STZ dose being 160 mg/kg body weight. Two-phase diabetes development was observed. Initial mild hypoinsulinemia and hyperglycemia turned to more severe diabetes after day 24 which was preceded by the first ICSA peak at day 13. The second ICSA peak occurred at day 35. The data obtained suggest that in this model of diabetes the toxic STZ effect induces both the diabetic syndrome and humoral autoimmunity to beta-cells, and the latter leads to further impairment of diabetes.

Animals↗
PubMedDate not supplied

[Comparative study of physico-chemical and biological properties of human somatotropin produced by genetic engineering and isolated from the pituitary gland].

Human somatotropin hormono (STH), produced by means of gene engineering in the complex program "Human growth hormone", managed by the Academy of Sciences of the USSR, Ministry of Medical and Biological Industry of the USSR and Ministry of Public Health of the USSR, was shown to be similar in its physico-chemical properties to the main isoform of highly purified STH, isolated from human hypophysis. As distinct from the hypophyseal STH (STHhyp) containing minor isoforms of the hormone, the preparation of biosynthetic STH (des-Phe1-STH; STHbio) proved to be homogeneous. Studies of biological properties showed that STHbio exhibited high, similar to STHhyp, immunological, growth-stimulating and insulin-like activities as well as it possessed the lipotropic effect in vivo. The lipotropic effect of STHbio in vivo was less prolonged as compared with that of STHhyp, while in vitro it was only slightly expressed in isolated rabbit fat tissue. The effect did not depend on the hormone dose, apparently due to either absence of the hormone modified forms in the STHbio preparation or other hypophyseal contaminating substances responsible for the lipotropic activity. STHbio, similarly to STHhyp, did not stimulate DNA synthesis in blood serum-free culture of human fibroblasts. Studies of STHbio biological properties suggest that multifunctionality of native STHhyp appear to depend on intrinsic specificity of its molecule.

Adipose Tissue↗