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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
1998-1-27
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pubmed:abstractText |
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl) labeled Na+/K+-ATPase covalently with two different inactivation constants (Ki = 2.5 microM; Ki' = 10 microM). It apparently modified the two different ATP-binding sites of the enzyme since it decreased the activity of the E2ATP site, i.e. the K+-activated para-nitrophenylphosphatase activity, in an enzyme whose high-affinity E1ATP site had been blocked by fluorescein 5'isothiocyanate (FITC). It also reduced the activity of the E1ATP site, i.e. the Na+-activated protein phosphorylation, in an enzyme whose low-affinity E2ATP site had been blocked by Co(NH3)4PO4. Fluorescence quenching experiments with KI, CsCl and MnCl2 of the NBD-Cl-labeled Na+/K+-ATPase revealed two differently accessible types of fluorophores depending on the ATP site: The E2ATP site apparently differs from the E1ATP site in that it is more open because the fluorophore labeling in the E2ATP site was sterically better accessible for quenchers.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-Chloro-7-nitrobenzofurazan,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
419
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
227-30
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading | |
pubmed:year |
1997
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pubmed:articleTitle |
Quenching of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole-modified Na+/K+-ATPase reveals a higher accessibility of the low-affinity ATP-binding site.
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pubmed:affiliation |
Institute of Physiology, Academy of Sciences of the Czech Republic, Prague.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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