| pubmed-article:2835083 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C0017687 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C0007448 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2835083 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:2835083 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2835083 | pubmed:dateCreated | 1988-6-14 | lld:pubmed |
| pubmed-article:2835083 | pubmed:abstractText | The effects of Mg2+ or ethylenediaminetetraacetic acid (EDTA) on 125I-glucagon binding to rat liver plasma membranes have been characterized. In the absence of guanosine 5'-triphosphate (GTP), maximal binding of 125I-glucagon occurs in the absence of added Mg2+. Addition of EDTA or Mg2+ diminishes binding in a dose-dependent manner. In the presence of GTP, maximal binding occurs in the presence of 2.5 mM Mg2+ (EC50 = 0.3 mM) while EDTA or higher concentrations of Mg2+ diminish binding. Response to exogenous Mg2+ or EDTA depends on the concentration of Mg2+ in the membranes and may vary with the method used for membrane isolation. Solubilized 125I-glucagon-receptor complexes fractionate on gel filtration columns as high molecular weight, GTP-sensitive complexes in which receptors are coupled to regulatory proteins and lower molecular weight, GTP-insensitive complexes in which receptors are not coupled to other components of the adenylyl cyclase system. In the absence of GTP, 40 mM Mg2+ or 5 mM EDTA diminishes receptor affinity for hormone (from KD = 1.2 +/- 0.1 nM to KD = 2.6 +/- 0.3 nM) and the fraction of 125I-glucagon in high molecular weight receptor-Ns complexes without affecting site number (Bmax = 1.8 +/- 0.1 pmol/mg of protein). Thus, while GTP promotes disaggregation of receptor-Ns complexes, Mg2+ or EDTA diminishes the affinity with which these species bind hormone. In the presence of GTP, hormone binds to lower affinity (KD = 9.0 +/- 3.0 nM), low molecular weight receptors uncoupled from Ns.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:2835083 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2835083 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2835083 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2835083 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2835083 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2835083 | pubmed:author | pubmed-author:DonnerD BDB | lld:pubmed |
| pubmed-article:2835083 | pubmed:author | pubmed-author:LipsonK EKE | lld:pubmed |
| pubmed-article:2835083 | pubmed:author | pubmed-author:MakiR GRG | lld:pubmed |
| pubmed-article:2835083 | pubmed:author | pubmed-author:KolhatkarA... | lld:pubmed |
| pubmed-article:2835083 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2835083 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:2835083 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:2835083 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2835083 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2835083 | pubmed:pagination | 1111-6 | lld:pubmed |
| pubmed-article:2835083 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
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| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:meshHeading | pubmed-meshheading:2835083-... | lld:pubmed |
| pubmed-article:2835083 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2835083 | pubmed:articleTitle | Divalent cations regulate glucagon binding. Evidence for actions on receptor-Ns complexes and on receptors uncoupled from Ns. | lld:pubmed |
| pubmed-article:2835083 | pubmed:affiliation | Memorial Sloan-Kettering Cancer Center, New York, New York 10021. | lld:pubmed |
| pubmed-article:2835083 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2835083 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
