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Pankov YuA

Publications and source records attributed to Pankov YuA.

12 recordsLinked to original sources
PubMed1997

On fundamental endocrinology.

Analysis is presented discussing why there is an absence of fundamental endocrinology in Russian science. Features of the session of the Academy of Sciences and the Lenin All-Union Academy of Agricultural Sciences (1948) and of the session of the Academy of Sciences and Academy of Medical Sciences (1950) and their influence on the development of science are considered. The less infamous Pavlov's session (1950) has had a more destructive influence on the development of endocrinology than Michurin's session has on the development of genetics. The prospects for development in Russia of fundamental endocrinology as of a branch of matrix biology are estimated pessimistically. At present, endocrinology has become a general biological science about hormones as the main regulators of vital processes. Specific hormones are generated by all organs, tissues, and cells of living organisms, functioning as means for communication between organs and tissues, and together with the nervous system unite them into a single whole.

Endocrinology↗
PubMed1986

Multiple forms of pituitary prolactin, a glycosylated form of porcine prolactin with enhanced biological activity.

Three forms of prolactin differing in molecular weight (Mr 23,000, 25,000 and 50,000, respectively) and electrophoretic mobility have been isolated and purified from fresh-frozen porcine pituitary glands. The prolactin form with Mr 25,000 is identified as a glycoprotein having an affinity to concanavalin A. The carbohydrate unit containing GlcNAc3, GalNAc1, Man3, Fuc 0.5, Gal 0.4 is linked to asparagine at the 31 position. The amino acid composition and partial primary structure of the glycosylated prolactin are identical to those of the major prolactin form (Mr 23,000). Based on isoelectric focusing and nondenaturing disc-electrophoresis, the glycosylated prolactin appears more acidic than the major form. The glycosylated form of the hormone has 140% of the activity of the non-glycosylated prolactin when measured by the pigeon crop sac assay. The new form accounts for 30-40% of the total monomeric prolactin in the porcine pituitary. The yield was 200 mg purified glycosylated prolactin from 1000 g pituitary gland. The third form of hormone (Mr 50,000) was shown to be a disulphide linked prolactin dimer.

Amino Acid Sequence↗
PubMed1986

Primary structure of sperm whale luteinizing hormone.

Luteinizing hormone was extracted from sperm whale pituitaries and separated into alpha- and beta-subunits. These subunits were cleaved with cyanogen bromide, and digested with trypsin and chymotrypsin. The fragments obtained were separated and purified by gel filtration on Sephadex and by ion exchange chromatography, reversed phase chromatography and chromatoelectrophoresis. The amino acid sequence of peptides obtained was studied by dansyl-Edman's method and Edman's modification of Chang et al. The study made it possible to establish the complete amino acid sequence of sperm whale LH alpha- and beta-subunits.

Amino Acid Sequence↗
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↗
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

Structural and functional organization of some pituitary protein hormones.

Some recent observations on the interrelation between structural and functional organization of some anterior pituitary hormones (corticotropin, beta-lipotropin, prolactin and somatotropin) made in this Institute are reviewed. The primary structure and interspecies differences of these hormones are discussed and a mathematical method of comparative analysis of the homologous amino acid sequences, which has been previously developed, is presented. A hypothesis has been raised that some sequences of the amino acid chains are closely related to the nature of biological effect of the appropriate protein hormone, while some other parts of the molecular are responsible predominantly for a contact with a specific receptor and several experimental data are presented which seem to be in agreement with such a view. This may be also supported by the observations that the lipolytic effect of somatotropin may be blocked by proteinase inhibitors (trasylol and methylamine) which shows that such an action presumably takes place only after a cleavage of its molecule by proteolytic enzymes into smaller fragments.

Adrenocorticotropic Hormone↗
PubMed1981

Accelerated method for comparing amino acid sequences with allowance for possible gaps. Plotting optimum correspondence paths.

An accelerated method is suggested which enables an effective comparison to be made of amino acid (nucleotide) sequences of great length with due regard to a large number of possible gaps. The method consists in limiting the area of complete similarity charts, calculated in accordance with the algorithm suggested by Sankoff (1972), by a certain specially selected diagonal band. The application of the Monte-Carlo method permits a statistical evaluation to be made of the certainty of the similarity of the compared sequences and to choose on such a "comparison band", an optimum "correspondence path" which can readily be transformed into sequence alignment. Using this approach, prolactin and somatotropin families of sequences were found to be homologous at a high level of significance and their optimum alignment with two gaps has been suggested. In contrast, two regions of assumed partial gene duplication in beta-galactosidase sequence, suggested by Hood et al. (1978), were found not to be statistically significantly similar.

Amino Acid Sequence↗
PubMedDate not supplied

Participation of beta-endorphin in the regulation of conditioned reflex activity of cats.

The role of beta-endorphin in the regulation of conditioned instrumental food-procuring reactions and more complex forms of nervous activity such as reflexes of choice of the side of reinforcement was studied in cats. It was established that the subcutaneous injection of small doses of beta-endorphin (10 micrograms/kg, 15 x 10(-6) micrograms/kg) exerts a facilitatory nonspecialized effect on positive and negative food-procuring conditioned reflexes that has an overall adaptive character overall. The influence of the same doses of beta-endorphin on conditioned reflexes of choice is more complex in character, depending upon the initial level of conditioned reflex activity and on the typological features of the experimental animals. A possible mechanism of the influence of beta-endorphin on higher nervous activity is discussed.

Animals↗