Wyniki wyszukiwania - AGRO

1

Single-strand conformation polymorphism within the porcine growth hormone gene promoter

100%

Kaminski S., Wachek M.

Animal Science Papers and Reports

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2002

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tom 20

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nr 1

2

Changes in insulin level and growth hormone in lambs blood caused by adding blood meal and dry brown livex [modified by whey] to forage

100%

Zawadzki W., Borodulin-Nadzieja L.

Polish Journal of Veterinary Sciences

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1998

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tom 01

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nr 1

The goal of this study was the assessment of the influence on both insulin and growth hormone levels in lambs blood of blood meal and Wroclaw product - dry brown livex (modified by whey). Experiments were carried out on 30 young Polish "wielkopolska" lowland - sheep - wool type, aged 3-4 months. Livex and blood meal constituted 2% of forage. Blood samples for radioimmunologic examinations (GH and insulin level determination) were taken 1 hour before feeding, directly before feeding and 1.0, 1.5, 2.0, 3.0, 5.0, 6.0 and 8.0 hours afterwards. During the experiment higher levels of insulin and GH were observed in animals fed with livex and forage mixture than in animals fed with blood meal and forage mixture. Livex caused a bigger body mass increase (mean increase 27.3%) in comparison with animals fed with control forage. Although neither livex nor blood meal are hormone preparations, changes in insulin and growth hormone levels were observed.

3

Examination of growth hormone (GH) gene polymorphism and its association with body weight and selected body dimensions in ducks

86%

Mazurowski A., Frieske A., Kokoszynski D., Mroczkowski S., Bernacki Z., Wilkanoska A.

Folia Biologica

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2015

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tom 63

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nr 1

4

Growth hormone gene polymorphism in chicken divergently selected for axial skeleton malformation

86%

Wardecka B., Jaszczak K., Parada R., Korczak M., Zieba G.

Journal of Animal and Feed Sciences

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2005

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tom 14

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nr 3

561-570

5

Insulin-like growth factor 1

86%

Gronek P., Rychlewski T., Slomski R., Stankiewicz K., Lehmann J.

Studies in Physical Culture and Tourism

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2005

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tom 12

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nr 1

6

Growth hormone gene expression in oocytes and zygotes produced by cows heterozygous (Leu127Val) at GH locus

86%

Warzych E., Namysl J., Kubiatowicz M., Lechniak D.

Reproductive Biology

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2004

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tom 04

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nr 3

7

Effect of pre-treatment and post-treatment of growth hormones [kinetine and abscisic acid] on germination and growth of fodderbeet and seabeet under saline soil conditions

86%

Niazi B. H., Rozema J., Athar M.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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2002

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tom 50

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nr 4

8

Effects of growth hormone on neuroendocrine function

86%

Bartke A., Chandrashekar V., Steger R. W.

Acta Neurobiologiae Experimentalis

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1996

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tom 56

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nr 3

9

Effect of the plant growth hormones on somatic embryogenesis of Gentiana sp. in cell suspension culture

86%

Mikula A., Wibik W., Rybczynski J. J.

Acta Physiologiae Plantarum

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1997

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tom 19

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nr 2

10

Growth rate and carcass quality in relation to GH-MspI and GH-HaeII PCR-RFLP polymorphism in pigs

86%

Pierzchala M., Blicharski T., Kuryl J.

Animal Science Papers and Reports

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2004

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tom 22

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nr 1

The objective of this study was to investigate the effect of two single nucleotide polymorphisms iIn growth hormone (GH) gene on performance traits in pigs. The animals (n= 320) belonged to four groups of commercial crosses being the progeny of crossbred Polish Landrace × Polish Large White sows and Polish Landrace, Polish Large White, Duroc or Pietrain boars. Genotypes of growth hormone gene (GH) were established with PCR-RFLP technique using MspI and HaeII endonucleases.The GH/MspI and GH/HaeII genotypes were found significantly related to the weight of ham, Wright of ham meat and ham content of carcass. Moreover, nearly significant differences between GH/MIPS genotypes were found for mean fat thickness (from five measurements), fat thickness at lower back (point K2) and over the loin, and for loin eye height. The results presented allow to assume that near the analysed mutation the QTLs for performance traits in pigs are located.

11

Tryptic digestion of peptides corresponding to modified fragments of human growth hormone-releasing hormone

86%

Witkowska E., Orlowska A., Izdebski J.

Acta Biochimica Polonica

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2004

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tom 51

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nr 1

The objective of this study was to examine the degradation of short peptides corresponding to modified fragments of human growth hormone-releasing hormone by trypsin. Six analogues of pentapeptide 9-13 of human growth hormone-releasing hormone containing homoarginine, ornithine, glutamic acid, glycine, leucine or phenylalanine residue in position 11, two analogues of hexapeptide 8-13 of human growth hormone-releasing hormone and two analogues of heptapeptide 7-13 of human growth hormone-releasing hormone containing homoarginine or glycine residue in position 11 were obtained. The peptides were subjected to digestion by trypsin and the course of reaction was monitored using HPLC. It was found that the rate of hydrolysis of the Lys12-Val13 peptide bond depends on the amino-acid residue preceding Lys12 . The extension of the peptide chain towards the N-terminus by introduction of consecutive amino-acid residues corresponding to the human growth hormone-releasing hormone sequence accelerates the hydrolysis process. These results may be of assistance in designing new analogues of human growth hormone-releasing hormone, more resistant to the activity of proteolytic enzymes.

12

Associations of growth hormone [GH] and prolactin [PRL] genes polymorphisms with milk production traits in Polish Black-and-White cattle

86%

Dybus A.

Animal Science Papers and Reports

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2002

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tom 20

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nr 4

13

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Performance of transgenic pigs produced with the use of two different growth hormone gene constructs

86%

Rozycki M., Smorag Z., Kopchick J. J., Chen W. Y., Jura J., Pasieka J., Orzechowska B., Gajda B., Skrzyszowska M.

Journal of Applied Genetics

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1999

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tom 40

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nr 1

14

Human pituitary adenoma cells and VIP. In vitro studies

86%

Fazekas I., Varga I., Bacsy E., Slowik F., Balint K., Pasztor E., Glaz E.

Folia Histochemica et Cytobiologica. Supplement

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1997

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tom 35

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nr 2

15

Fine-structural and immunocytochemical analysis of human somatotropic and mammotropic adenoma cell cultures

86%

Bacsy E., Fazekas I., Pasztor E.

Folia Histochemica et Cytobiologica. Supplement

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1997

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tom 35

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nr 2

16

Optimization of carbon-nitrogen ratio for production of gibberellic acid by Pseudomonas sp.

86%

Basiacik K. S., Aksoz N.

Polish Journal of Microbiology

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2004

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tom 53

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nr 2

In this study, favorable carbon-nitrogen ratio for high yields of gibberellic acid (GA₃) production from Pseudomonas sp. was investigated. First of all, optimum carbon (glucose, maltose, sucrose, fructose, lactose) and nitrogen (KNO₃, NH₄C1, NaNO₃, urea, glycine) sources among the others were chosen. The highest yield of GA₃ productivity was found in growth medium supplemented with fructose (168.5 mg/L). NaNO₃ was found as a suitable nitrogen source (141 mg/L). Then, in order to determine the optimum carbon-nitrogen ratio, different concentrations of carbon (from 50 mM to 150 mM) and nitrogen (from 17 mM to 47 mM) sources were added in culture media. As a result, optimum carbon-nitrogen ratio for GA₃ production from Pseudomonas sp. was found to be 100:17 mM.

17

Polymorphism of the porcine growth hormone gene and its linkage to microsatellites S0083 and S0090

86%

Korwin-Kossakowska A., Pierzchala M., Kuryl J., Zwierzchowski L., Cymerowska-Prokopczyk I., Siadkowska E.

Journal of Applied Genetics

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1999

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tom 40

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nr 2

18

Treatment of systemic diseases by inhalation of biomolecule aerosols

72%

Siekmeier R., Scheuch G.

Journal of Physiology and Pharmacology. Supplement

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2009

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tom 60

|

nr 5

19

Expression of the growth hormone gene in the chicken during embryonic and posthatch development

72%

Grossmann R., Muhlbauer E., Ellendorff F., Jozsa R., Reiprich K.

Zeszyty Naukowe. Przegląd Hodowlany

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1997

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tom 31

20

The role of orexin A in the control of prolactin and growth hormone secretions in sheep - in vitro study

72%

Molik E., Zieba D. A., Misztal T., Romanowicz K., Wszola M., Wierzchos E., Nowakowski M.

Journal of Physiology and Pharmacology. Supplement

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2008

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tom 59

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nr 9

91-100

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