| pubmed-article:2177321 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2177321 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:2177321 | lifeskim:mentions | umls-concept:C0025234 | lld:lifeskim |
| pubmed-article:2177321 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:2177321 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:2177321 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:2177321 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:2177321 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2177321 | pubmed:dateCreated | 1991-2-28 | lld:pubmed |
| pubmed-article:2177321 | pubmed:abstractText | The (Na+ + K+)ATPase is inhibited by the bee venom polypeptide, melittin. KCl and NaCl protect the enzyme from melittin inhibition. Analysis of the K+ and Na+ protection against melittin inhibition suggested a kinetic model which was consistent with slowly reversible melittin binding, and mutually exclusive binding of melittin with K+ and Na+. Accordingly, in the absence of salt, the KI for melittin inhibition = 1.2 microM, and the protection by KCl occurs with a KA,KCl = 0.6 mM. The protection by NaCl occurs with a KA,NaCl = 15 mM. Melittin inhibition of enzyme activity is due to direct interactions with the (Na+ + K+)ATPase, as demonstrated by photolabeling with [125I]azidosalicylyl melittin, which labeled the alpha subunit, but not the beta subunit of the (Na+ + K+)ATPase. Melittin and KCl reduced the extent of labeling. In non-covalent binding studies using [125I]azidosalicylyl melittin, the stoichiometry of binding was 1.6 melittin per (Na+ + K+)ATPase. Ligand-induced conformational changes of FITC-labeled (Na+ + K+)ATPase were examined in the presence and absence of melittin. K+ alone or melittin alone caused a fluorescence intensity quenching consistent with formation of an E2 form of the enzyme. The NaCl-induced (E2----E1) fluorescence intensity changes were maximal when the enzyme was treated with K+. NaCl-induced fluorescence changes did not occur when the enzyme was treated with melittin in the absence of K+. However, when K+ was present before the addition of melittin, NaCl-induced fluorescence intensity increases were observed, which were dependent upon the concentration of K+ in the preincubation mixture. The results of the labeling and conformational studies support the kinetic model and suggest a mechanism for inhibition of ion pumps by (poly)peptides. | lld:pubmed |
| pubmed-article:2177321 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2177321 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2177321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2177321 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2177321 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2177321 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:2177321 | pubmed:author | pubmed-author:CuppolettiJJ | lld:pubmed |
| pubmed-article:2177321 | pubmed:author | pubmed-author:AbbottA JAJ | lld:pubmed |
| pubmed-article:2177321 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2177321 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:2177321 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2177321 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2177321 | pubmed:pagination | 249-57 | lld:pubmed |
| pubmed-article:2177321 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
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| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:meshHeading | pubmed-meshheading:2177321-... | lld:pubmed |
| pubmed-article:2177321 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2177321 | pubmed:articleTitle | Interaction of melittin with the (Na+ + K+)ATPase: evidence for a melittin-induced conformational change. | lld:pubmed |
| pubmed-article:2177321 | pubmed:affiliation | Department of Physiology and Biophysics, University of Cincinnati College of Medicine, Ohio 45267-0576. | lld:pubmed |
| pubmed-article:2177321 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2177321 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2177321 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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