Nuclcotide sequence of the growth hormone gene cDNA from goat<i>Copra hircus</i>L. (Tokara)

Yato, Miki; Yamano, Yoshiaki; Oyabayashi, Kazuo; Okuno, Mitsuhiro; Kioka, Noriyuki; Manabe, Eichi; Hashi, Hidetaka; Sakai, Hiroshi; Komano, Tohru; Utsumi, Kyozo; Iritani, Akira

doi:10.1093/nar/16.8.3578

Cited by 13 publications

(7 citation statements)

References 1 publication

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“…The sequence of goat pituitary GH cDNA was reported by Yamano et al (1988) and Yato et al (1988) and the GH gene sequence was described by Kioka et al (1989). The coding sequence predicted from the gene sequence corresponds to the goat GH cDNA sequence and this gene was subsequently shown to be the gGH1 gene.…”

Section: Sequence Studiesmentioning

confidence: 99%

Duplicate growth hormone genes in sheep and goat

Wallis¹,

Lioupis²,

Wallis³

1998

Journal of Molecular Endocrinology

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Section: Sequence Studiesmentioning

confidence: 99%

Duplicate growth hormone genes in sheep and goat

Wallis¹,

Lioupis²,

Wallis³

1998

Journal of Molecular Endocrinology

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“…Growth hormone (GH) is a polypeptide chain which is involved in a number of anabolic processes (Wallis, 1985). A number of reports are available on the primary structure, gene cloning and expression of growth hormone gene (Santome, 1971;Sami, 2006;Sereikeite, 2007;Wallis, 1973Wallis, , 1985Wallis, , 2001Wallis, , 2005Wallis, , 2006Verma, 1999;Yato, 1988;Vize, 1987). GH gene in ruminants comprised of 2.1 KB present at chromosome 19.…”

Section: Introductionmentioning

confidence: 99%

Deletion of amino acid residues 33-46 in growth hormone alters the hydrophobicity of the molecule

Sami¹

2010

Afr. J. Biotechnol.

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Growth hormone (GH) variants have been studied for the structure-function relationship of the molecule. The presence of a potential alternate splicing point in mRNA in bGH gene at exon 3, similar to hGH has been reported by workers. Early investigation on the characteristics of the chemistry of 20k oGH showed that the molecule was produced by site-directed mutagenesis by deleting amino acid residues 33-46 and the resultant DNA was expressed in E. coli under the control of lac promoter in pUC based plasmid. The mutant protein remained insoluble and did not refold. To investigate the effect of deletion on the chemistry of the molecule, computational biology tools were employed. The mutant with the deletion of amino acid residues 33-46, was designed and the model was visualized on computer. The structure of 20k bGH was compared with bGH and dissected for hydrogen bonds and hydrophobicity. Computational biology tools were helpful in elucidating the role of 33-46 amino acid residues domain in the chemistry of the molecule. Furthermore, it was revealed that removal of amino acid residues 33-46 which formed the hydrogen bonds involving Glu 33, Gln 46, Pro 38, Arg 42, Tyr 43,Ala 51, Thr 48, Asn 47, led to the formation of new hydrogen bonds between Thr 33, Tyr 144, Asn 32, Asn 32 and Ser and Asp 153. The removal of the amino acids 33-46 decreased the hydro-phobicity of the first helix of bGH molecule, as compared to 20k hGH, thus altering the solubility of the molecule, confirming the earlier reported results for ovine growth hormone with same deletion.

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“…GH binds with two receptor molecules to exhibit its biological activity (de Vos et al, 1992). Gene for GH expression and peptide has been isolated, purified and chatecterised from different farm animals including bubaline, bovine, ovine, porcine and caprine origin (Sami, 2006;Verma et al, 1999;Schoner, 1985;Wallis, 1973;Yato, 1988;Warick et al, 1989;Vize et al, 1987). A number of reports are available on the cloning and sequencing of GH gene.…”

Section: Introductionmentioning

confidence: 99%

Production, purification and characterization of two recombinant DNA-derived N-terminal ovine growth hormone variants: oGH3 and oGH5

Amtul¹,

Wallis²

2008

Afr. J. Biotechnol.

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Two recombinant DNA-derived variants of ovine growth hormone were produced, purified, characterized and compared with the authentic pituitary derived GH. The variants oGH3 and oGH5 were isolated by differential centrifugation method and were purified after refolding by ion-exchange chromatography and gel filtration. Both the proteins showed single band on SDS-PAGE and had molecular weight and iso-electric point closer to authentic pituitary GH. The variants oGH3 and oGH5 were compared with the authentic pituitary derived GH in radio immuno assays, radio receptor assays and binding with the monoclonal antibodies OA 11 and OA12.

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Nuclcotide sequence of the growth hormone gene cDNA from goatCopra hircusL. (Tokara)

Cited by 13 publications

References 1 publication

Duplicate growth hormone genes in sheep and goat

Duplicate growth hormone genes in sheep and goat

Deletion of amino acid residues 33-46 in growth hormone alters the hydrophobicity of the molecule

Production, purification and characterization of two recombinant DNA-derived N-terminal ovine growth hormone variants: oGH3 and oGH5

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