A radioimmunoassay of chicken growth hormone using growth hormone produced by recombinant DNA technology : validation and observations of plasma hormone variations in genetically fat and lean chickens

Picaper, G.; Leclercq, B.; Saadoun, A.; Mongin, P.

doi:10.1051/rnd:19860703

Cited by 14 publications

(4 citation statements)

References 9 publications

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“…The antiserum showed no cross-reactivity to two different chicken prolactin preparations nor to ovine prolactin. It does not cross-react with either ovine or rat GH and be¬ haves in our laboratory in a manner very similar to that reported by Picaper et al (1986).…”

Section: Methodssupporting

confidence: 85%

“…Samples (20 pi) of the pituitary homogenates were injected. cGH in the HPGPC frac¬ tions was measured by radioimmunoassay using a rabbit antiserum raised against cDNA-derived cGH with cDNA-derived cGH as standard and tracer (Picaper, Leclercq, Saadoun & Mongin, 1986). The sensitivity of the assay, defined as the concentration resulting in a response 2-5 standard deviations away from the zero dose-response was 2-2 pg/1 (n = 20).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Molecular forms of growth hormone in the chicken pituitary gland

Houston¹,

Goddard²

1988

Journal of Endocrinology

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Different forms of GH present in freshly prepared homogenates of chicken pituitary were analysed by high-performance gel permeation chromatography and by immunoblotting following sodium dodecylsulphate polyacrylamide gel electrophoresis, nondenaturing polyacrylamide gel electrophoresis and isoelectric focussing. Chicken GH was found to occur mainly in a monomeric form with a relative molecular mass of 23,500 together with small amounts of interchain disulphide-linked oligomers. No evidence was obtained for proteolytically modified forms of GH nor for a form analogous to the 20K variant of human GH. Isoelectric focussing resolved ten distinct charge variants of chicken GH with isoelectric points between 8.45 and 6.0. The predominant charge variant (pI = 7.85) was present in pituitaries of birds of both sexes at all ages examined (3-114 days) whereas the more acidic forms were not apparent until after day 13. These findings indicate that the chicken pituitary contains different forms of GH, some of which may be developmentally regulated.

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Section: Methodssupporting

confidence: 85%

Section: Methodsmentioning

confidence: 99%

Molecular forms of growth hormone in the chicken pituitary gland

Houston¹,

Goddard²

1988

Journal of Endocrinology

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“…In 5-week-old birds from generation F9, fasted for 16 h and then refed, the plasma growth hormone (GH) concentration was higher in FL than in LL (Picaper et al, 1986). In contrast, Williams et al (1986) found no differences between the lines for GH or oestradiol plasma concentrations measured from 6 to 24 weeks of age in fed female birds of the F4 generation.…”

Section: Other Hormonesmentioning

confidence: 97%

Chicken lines divergent for low or high abdominal fat deposition: a relevant model to study the regulation of energy metabolism

Baéza¹,

Bihan-Duval²

2013

Animal

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Divergent selection of chickens for low or high abdominal fat (AF) but similar BW at 63 days of age was undertaken in 1977. The selection programme was conducted over seven successive generations. The difference between lines was then maintained constant at about twice the AF in the fat line as in the lean line. The aims of the first studies on these divergent chicken lines were to describe the growth, body composition and reproductive performance in young and adult birds. The lines were then used to improve the understanding of the relationship between fatness and energy and protein metabolism in the liver, muscle and adipose tissues, as well as the regulation of such metabolism at hormonal, gene and hypothalamic levels. The effects on muscle energy metabolism in relation to meat quality parameters were also described. This paper reviews the main results obtained with these lines.

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“…Existing assays for the determination of GH in fowl blood samples are mainly based on homologous and heterologous radioimmunoassay ( RIA ) using native GH protein extracted from a large number of pituitary glands ( Harvey and Scanes, 1977 ; Proudman and Wentworth, 1978 ; Leung et al, 1984 ; Zheng et al, 2007 ) or recombinant avian GH ( Proudman, 1984 ; Picaper et al, 1986 ). However, RIA requires the use of hazardous radioisotopes that restrict assay use to specialized laboratories.…”

Section: Introductionmentioning

confidence: 99%

Research Note: Development of a sandwich ELISA for determining plasma growth hormone concentrations in goose

et al. 2022

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Growth hormone ( GH ) is required for normal postnatal development in poultry; however, no immunoassay exists to assess its levels in geese plasma, hindering the study of endocrine regulation in this species. We developed a sandwich ELISA to determine the GH concentrations in the plasma of geese. Recombinant goose GH was produced using a eukaryotic expression system and purified for use as the reference standard in ELISA and the antigen for producing the polyclonal antibodies in rabbits. Rabbit anti-goose GH polyclonal antibody was used to coat the wells of the ELISA plate, and its biotinylated form served as the detection antibody. An avidin-conjugated horseradish peroxidase was used to bind the detection antibody and catalyze the chromogenic reaction of 3,3,5,5-tetramethylbenzidine and H 2 O 2 . A sigmoidal curve was fitted to the optical density and the log of the standard GH concentration using the four-parameter logistic model. The sensitivity of the assay was less than 0.156 ng/mL. The intra- and interassay coefficients of variation were less than 9 and 13%, respectively. The response curve of the serially diluted plasma samples from geese exhibited a good parallel relationship with that observed for the reference standards. The assay effectively detected differences in GH concentrations in plasma samples from geese at various physiological stages; thus, it will be useful for future study of their growth and metabolism.

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A radioimmunoassay of chicken growth hormone using growth hormone produced by recombinant DNA technology : validation and observations of plasma hormone variations in genetically fat and lean chickens

Cited by 14 publications

References 9 publications

Molecular forms of growth hormone in the chicken pituitary gland

Molecular forms of growth hormone in the chicken pituitary gland

Chicken lines divergent for low or high abdominal fat deposition: a relevant model to study the regulation of energy metabolism

Research Note: Development of a sandwich ELISA for determining plasma growth hormone concentrations in goose

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