Binding properties of solubilized gonadotropin-releasing hormone receptor: role of carboxylic groups

Hazum, E

doi:10.1021/bi00396a023

Title: Binding properties of solubilized gonadotropin-releasing hormone receptor: role of carboxylic groups

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Abstract

The interaction of /sup 125/I-buserelin, a superactive agonist of gonadotropin-releasing hormone (GnRH), with solubilized GnRH receptor was studied. The highest specific binding of /sup 125/I-buserelin to solubilized GnRH receptor is evident at 4/sup 0/C, and equilibrium is reached after 2 h of incubation. The soluble receptor retained 100% of the original binding activity when kept at 4 or 22/sup 0/C for 60 min. Mono- and divalent cations inhibited, in a concentration-dependent manner, the binding of /sup 125/I-buserelin to solubilized GnRH receptor. Monovalent cations require higher concentrations than divalent cations to inhibit the binding. Since the order of potency with the divalent cations was identical with that of their association constants to dicarboxylic compounds, it is suggested that there are at least two carboxylic groups of the receptor that participate in the binding of the hormone. The carboxyl groups of sialic acid residues are not absolutely required for GnRH binding since the binding of /sup 125/I-buserelin to solubilized GnRH receptor was only slightly affected by pretreatment with neuraminidase and wheat germ agglutinin. The finding that polylysines stimulate luteinizing hormone (LH) release from pituitary cell cultures with the same efficacy as GnRH suggest that simple charge interactions can induce LH release. Accordingmore »« less

Authors:: Hazum, E

Publication Date:: Tue Nov 03 00:00:00 EST 1987

Research Org.:: Weizmann Inst. of Science, Rehovot (Israel)

OSTI Identifier:: 5513238

Resource Type:: Journal Article

Journal Name:: Biochemistry; (United States)

Additional Journal Information:: Journal Volume: 26:22

Country of Publication:: United States

Language:: English

Subject:: 62 RADIOLOGY AND NUCLEAR MEDICINE; LH; RADIOIMMUNOASSAY; LIBERINS; CONFIGURATION INTERACTION; RECEPTORS; ARGININE; GONADOTROPINS; IODINATION; IODINE 125; PITUITARY GLAND; AMINO ACIDS; BETA DECAY RADIOISOTOPES; BODY; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; ENDOCRINE GLANDS; GLANDS; HALOGENATION; HORMONES; IMMUNOASSAY; IMMUNOLOGY; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; MEMBRANE PROTEINS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANS; PEPTIDE HORMONES; PITUITARY HORMONES; PROTEINS; RADIOASSAY; RADIOIMMUNOLOGY; RADIOISOTOPES; TRACER TECHNIQUES; 550601* - Medicine- Unsealed Radionuclides in Diagnostics

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                    Hazum, E. Binding properties of solubilized gonadotropin-releasing hormone receptor: role of carboxylic groups.  United States: N. p., 1987. 
        Web.  doi:10.1021/bi00396a023.

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                    Hazum, E. Binding properties of solubilized gonadotropin-releasing hormone receptor: role of carboxylic groups.  United States.  https://doi.org/10.1021/bi00396a023

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                    Hazum, E. 1987.  
        "Binding properties of solubilized gonadotropin-releasing hormone receptor: role of carboxylic groups".  United States.  https://doi.org/10.1021/bi00396a023.

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@article{osti_5513238,

  title        = {Binding properties of solubilized gonadotropin-releasing hormone receptor: role of carboxylic groups},

  author       = {Hazum, E},

  abstractNote = {The interaction of /sup 125/I-buserelin, a superactive agonist of gonadotropin-releasing hormone (GnRH), with solubilized GnRH receptor was studied. The highest specific binding of /sup 125/I-buserelin to solubilized GnRH receptor is evident at 4/sup 0/C, and equilibrium is reached after 2 h of incubation. The soluble receptor retained 100% of the original binding activity when kept at 4 or 22/sup 0/C for 60 min. Mono- and divalent cations inhibited, in a concentration-dependent manner, the binding of /sup 125/I-buserelin to solubilized GnRH receptor. Monovalent cations require higher concentrations than divalent cations to inhibit the binding. Since the order of potency with the divalent cations was identical with that of their association constants to dicarboxylic compounds, it is suggested that there are at least two carboxylic groups of the receptor that participate in the binding of the hormone. The carboxyl groups of sialic acid residues are not absolutely required for GnRH binding since the binding of /sup 125/I-buserelin to solubilized GnRH receptor was only slightly affected by pretreatment with neuraminidase and wheat germ agglutinin. The finding that polylysines stimulate luteinizing hormone (LH) release from pituitary cell cultures with the same efficacy as GnRH suggest that simple charge interactions can induce LH release. According to these results, the authors propose that the driving force for the formation of the hormone-receptor complex is an ionic interaction between the positively charged amino acid arginine in position 8 and the carboxyl groups in the binding site.},

  doi          = {10.1021/bi00396a023},

  url          = {https://www.osti.gov/biblio/5513238},
  journal      = {Biochemistry; (United States)},
number       = ,

  volume       = 26:22,

  place        = {United States},

  year         = {Tue Nov 03 00:00:00 EST 1987},

  month        = {Tue Nov 03 00:00:00 EST 1987}

}

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