Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1987-3-13
|
| pubmed:abstractText |
The effects of lead (Pb) on the calmodulin activation of human red blood cell membrane calcium-dependent adenosine triphosphatase (Ca-ATPase) were studied in vitro. It was not possible to exclude EGTA from the hemolyzing buffer and retain Ca-ATPase activity and therefore exact concentrations of Pb in the incubation are not known. Nonetheless, nanomolar concentrations of Pb stimulated Ca-ATPase with or without exogenous calmodulin and none of the Pb concentrations tested (1 nM-100 microM) interfered with the calmodulin stimulation of the enzyme. High concentrations of Pb (greater than 10 microM) inhibited Ca-ATPase activity. It is possible that low concentrations of Pb can interfere with calcium dependent processes but the calcium-regulatory protein, calmodulin, is not susceptible to interference by Pb under the conditions used here.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0171-9750
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
9
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
397-400
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading | |
| pubmed:year |
1986
|
| pubmed:articleTitle |
Lead does not affect calmodulin-induced activation of calcium-dependent adenosine triphosphatase in human red blood cell membranes.
|
| pubmed:publicationType |
Journal Article,
In Vitro
|