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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1976-8-2
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pubmed:abstractText |
1. The chemical shifts (delta) of the phosphates of 2,3-diphosphoglycerate and adenosine triphosphate (ATP) were determined by phosphorus nuclear magnetic resonance (31P NMR) spectroscopy and were found to be displaced downfield following the addition of hemoglobin (3 mM) to a solution of either diphosphoglycerate (5 mM) or ATP (1 mM). 2. The binding of these compounds to hemoglobin was also determined by membrane ultrafiltration. A direct relationship was observed between the change in chemical shift ((delta delta) of the 2-P and 3-P of diphosphoglycerate and the percent diphosphoglycerate bound, when the latter was varied by altering pH, oxygenation state, or total diphosphoglycerate concentration. 3. In comparable studies with ATP binding, a linear relationship between the delta delta values of the gamma-, beta-, and alpha-P of ATP and the percent of ATP bound was not observed when the data from all of the experiments were plotted. NMR signals were not detectible in deoxyhemoglobin solutions containing 1 mM ATP but were seen in solutions containing 3.8 mM ATP. 4. The results indicate that 31P NMR spectroscopy is a promising tool for investigating organic phosphate interactions with hemoglobin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
427
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
481-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:5126-Adenosine Triphosphate,
pubmed-meshheading:5126-Binding Sites,
pubmed-meshheading:5126-Diphosphoglyceric Acids,
pubmed-meshheading:5126-Hemoglobins,
pubmed-meshheading:5126-Humans,
pubmed-meshheading:5126-Hydrogen-Ion Concentration,
pubmed-meshheading:5126-Kinetics,
pubmed-meshheading:5126-Magnetic Resonance Spectroscopy,
pubmed-meshheading:5126-Oxyhemoglobins,
pubmed-meshheading:5126-Protein Binding,
pubmed-meshheading:5126-Protein Conformation,
pubmed-meshheading:5126-Ultrafiltration
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pubmed:year |
1976
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pubmed:articleTitle |
Interactions between hemoglobin and organic phosphates investigated with 31P nuclear magnetic resonance spectroscopy and ultrafiltration.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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