Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1986-9-25
pubmed:abstractText
We have used several trivalent lanthanides as probes for the high-affinity Ca(II)-binding site of the Ca(II) + Mg(II)-ATPase of skeletal muscle sarcoplasmic reticulum. The luminescent probes Eu(III) and Tb(III) were excited directly with pulsed laser light and the energy transfer efficiencies to several lanthanide acceptors were measured, under conditions in which most donor-acceptor pair occupied high-affinity Ca(II) sites. We obtain an inter-ionic site distance of about 0.8-0.9 nm. Energy transfer measurements were also done with Eu(III) in at least one Ca(II) site and bidentate Cr-ATP complex at the ATP hydrolytic site. Quenching of Eu(III) luminescence by Cr-ATP was total under these conditions. We calculate an upper limit of 1.0 nm for the distance from the Ca(II) site(s) to the complexed Cr(III) ion at the hydrolytic site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
158
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
555-60
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Estimation of inter-binding-site distances in sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase using Eu(III) luminescence energy transfer.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.