Identification and partial purification of serum growth hormone binding protein in domestic animal species.
Abstract: The chemical nature and variations in serum concentrations of growth hormone binding protein (GHBP) from humans, rabbits, and rodents have been reported. To date little is known about the GHBP of domestic animals. Therefore, we initiated these studies to determine whether a serum GHBP was present in domestic animals and to purify the binding protein (BP) from serum of selected species. Using a dextran-coated charcoal separation assay, specific growth hormone (GH) binding was demonstrated in ovine, bovine, chicken, human, goose, porcine, and equine serum (listed in sequence from lowest to highest binding). Variation in BP activity was relatively high, both within and between species. Yearling ewes had higher serum GHBP than either prepubertal (4 mo) or older (5 yr) ewes. The GHBP was partially purified from chicken, ovine, and porcine serum using GH affinity chromatography. These BP had high affinity (Ka = 2 x 10(8) to 2 x 10(9) L/mol, depending on species) and low capacity (2 x 10(-10) to 5 x 10(-11) mol/unit of protein) for human GH but showed lower binding affinity for homologous GH (Ka = 2 x 10(7) L/mol). The porcine GHBP had the highest and ovine GHBP the lowest affinity for human GH. Other heterologous somatotropic hormones, ovine placental lactogen, and ovine GH displayed higher binding affinity to chicken and pig BP than the respective homologous hormones. Further chromatographic purification of the porcine GHBP resulted in an additional 1,000-fold purification. The estimated molecular weight of porcine GHBP is 50,000 to 60,000 Da. These results demonstrate that the serum from all domestic species tested contains a specific GH-binding moiety and that under the conditions described here human GH is a more efficient ligand than the homologous hormone.
Publication Date: 1992-03-01 PubMed ID: 1564002DOI: 10.2527/1992.703773xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study reveals the presence of growth hormone binding protein (GHBP) in domestic animals and partially purifies it from the serum of specific species. The study also highlights that the human growth hormone is a more efficient ligand than the equivalent hormone in these animals.
Objective of Research
- The primary objective of this research was to investigate the presence of growth hormone binding protein (GHBP) in domestic animals – a topic previously lacking in sufficient research.
- The research team aimed to partially purify this binding protein from the serum of different species, to study variations in serum concentrations and examine its nature and related chemical properties.
Methodology
- The study utilized a dextran-coated charcoal separation assay to demonstrate the specific binding of growth hormone (GH) in various species, namely ovine, bovine, chicken, human, goose, porcine, and equine serum, in ascending order of highest binding.
- The GHBP was then partially purified from the serum of selected species, such as chicken, ovine, and porcine, using growth hormone affinity chromatography.
- Inpects of the GHBP such as its affinity and capacity were then recorded for further analysis.
- The researchers also determined the estimated molecular weight of porcine GHBP.
Findings
- This research found significant variation in binding protein activity both within and between species. For instance, yearling ewes had higher serum GHBP concentrations than either prepubertal or older ewes.
- The purified GHBP revealed high affinity and low capacity for human GH but displayed lower binding affinity for homologous GH (GH from the same species).
- Notably, porcine GHBP had the highest affinity for human GH, while ovine GHBP had the lowest.
- Further purification of porcine GHBP resulted in an additional 1,000-fold purification, demonstrating it contains a high quantity of GHBP.
- The estimated molecular weight of the purified porcine GHBP was found to be between 50,000 to 60,000 Da.
- The results showed that the serum from all domestic species tested contained a specific GH-binding entity. Moreover, it was found that human GH was a more efficient ligand than homologous hormones.
Cite This Article
APA
Davis SL, Graf M, Morrison CA, Hall TR, Swift PJ.
(1992).
Identification and partial purification of serum growth hormone binding protein in domestic animal species.
J Anim Sci, 70(3), 773-780.
https://doi.org/10.2527/1992.703773x Publication
Researcher Affiliations
- Department of Animal Sciences, Oregon State University, Corvallis 97331.
MeSH Terms
- Animals
- Carrier Proteins / blood
- Carrier Proteins / isolation & purification
- Cattle / blood
- Chickens / blood
- Chromatography, Affinity
- Female
- Geese / blood
- Growth Hormone / metabolism
- Horses / blood
- Humans
- Male
- Sheep / blood
- Swine / blood
Citations
This article has been cited 2 times.- Beattie J, Phillips K, Shand JH, Brocklehurst S, Flint DJ, Allan GJ. Sensitivity of hybrid ovine/rat GH receptors to oGH and rat GH in transfected FDC-P1 mouse myeloid cells in vitro. Mol Cell Biochem 2002 Sep;238(1-2):137-43.
- Baumann G, Shaw MA, Amburn K. Circulating growth hormone binding proteins. J Endocrinol Invest 1994 Jan;17(1):67-81.
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