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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
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pubmed:dateCreated |
1985-3-11
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|
pubmed:abstractText |
The (Ca2+ + Mg2+)-ATPase from erythrocyte ghosts catalyzed the hydrolysis of ATP together with the synthesis of ATP or ATP in equilibrium 'Pi exchange. The modulation of the ATPase reaction cycle was controlled by high- and low-affinity calcium-binding sites asymmetrically located on the enzyme. Calmodulin accelerated the reaction cycle in both directions, stimulating the overall turnover of the enzyme. Calcium transport was achieved utilizing optimal conditions for the expression of the ATP in equilibrium Pi exchange system.
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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 |
Jan
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|
pubmed:issn |
0006-3002
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|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
10
|
|
pubmed:volume |
812
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
163-7
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|
pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
|
|
pubmed:year |
1985
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|
pubmed:articleTitle |
Synthesis of ATP catalyzed by the (Ca2+ + Mg2+)-ATPase from erythrocyte ghosts. Energy conservation in plasma membranes.
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|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
