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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1985-10-21
|
| pubmed:abstractText |
Calcium binding to calcium-dependent ATPase purified from erythrocyte membrane was assessed by measurements of the ATPase intrinsic fluorescence. Calcium-binding isotherms obtained by fluorescence titration are identical to curves representing the Ca2+-concentration dependence of ATPase activity, and demonstrate that cooperativity is in fact a feature of the binding mechanism rather than an apparent effect of enzyme kinetics. Loss of cooperativity and a reduction of the ATPase affinity for calcium is observed at very low enzyme concentrations. This effect of enzyme dilution is prevented by calmodulin at 37 degrees C but not at 25 degrees C. It is suggested that calcium binding by erythrocyte-membrane ATPase is influenced by hydrophobic interactions of binding domains, exhibiting a dissociation constant between 10(-7) and 10(-8) M in the absence of calmodulin, at 37 degrees C and in a specific set of experimental conditions. The dissociation constant is decreased by calmodulin.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0014-5793
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
9
|
| pubmed:volume |
189
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
67-71
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading | |
| pubmed:year |
1985
|
| pubmed:articleTitle |
Cooperative calcium binding and calmodulin regulation in the calcium-dependent adenosine triphosphatase purified from the erythrocyte membrane.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|