Induction of specific human growth hormone binding sites in rat liver by human growth hormone.
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چکیده
منابع مشابه
A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone
A binding study of nickel ions by a new recombinant human Growth Hormone (hGH), produced as an injected drug, has been done at 27˚C in NaCl solution (50 mM) using an isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for nickel ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 40 μM and -16...
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The interaction of hGH with some metal ions ( ) at 27°C in NaC1 solution, 50 mM was studied using Isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for binding of all these metal ions, expect . The intrinsic association equilibrium constants () are not very different for and , and also their molar enthalpies of binding (KJ/mol for and KJ/mo...
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Growth hormone secretagogue binding sites in peripheral human tissues.
The family of GH secretagogues (GHS) includes peptidyl (hexarelin) and nonpeptidyl (MK 0677) molecules possessing specific receptors in the brain, pituitary, and thyroid. GHS receptor subtypes have also been identified in the heart; and a gastric-derived peptide, named ghrelin, has recently been proposed as a natural ligand. Our aim was to investigate the presence of GHS receptors in a wide ran...
متن کاملSpecific binding sites for synthetic growth hormone secretagogues in non-tumoral and neoplastic human thyroid tissue.
The presence of specific receptors for synthetic growth hormone secretagogues (GHSs) has been investigated in non-tumoral and neoplastic human thyroid tissue using a radio-iodinated peptidyl GHS ((125)I-labelled Tyr-Ala-hexarelin) as ligand. Specific binding sites for Tyr-Ala-hexarelin were detected in membranes from non-tumoral and follicular-derived neoplastic thyroid tissue, but not in thyro...
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ژورنال
عنوان ژورنال: Endocrinologia Japonica
سال: 1979
ISSN: 0013-7219,2185-6370
DOI: 10.1507/endocrj1954.26.523