Linked Life Data

1388154

Source:http://linkedlifedata.com/resource/pubmed/id/1388154

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1992-10-19
pubmed:abstractText
Rate constants for most of the steps of the reaction cycle of the sarcoplasmic reticulum calcium-ATPase are similar or identical with Ca2+ or Sr2+ as the transported ions in spite of the large differences in the size and affinity of Ca2+ and Sr2+ (5 mM MgCl2, 100 mM KCl, pH 7.0, 25 degrees C). Phosphorylation of cE.Sr2 and cE.Ca2 by ATP occurs with kp = 220-235 s-1, whereas phosphorylation of E.ATP+Ca2+ or Sr2+ is consistent with kb = 50-70 s-1. Hydrolysis of E approximately P.Sr2 and E approximately P.Ca2 occurs with kt = 20 s-1, and the addition of 7 mM ADP to E approximately P.Sr2 or to E approximately P.Ca2 gives a burst of approximately 43% dephosphorylation, followed by dephosphorylation with k = 46 s-1. However, one Sr2+ ion dissociates from cE.Sr2 and from cE.ATP.Sr2 with k congruent to 120 s-1, whereas one Ca2+ ion dissociates from cE.Ca2 with k = 38 s-1 and from cE.ATP.Ca2 with k = 80 s-1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18466-74
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
The kinetics for the phosphoryl transfer steps of the sarcoplasmic reticulum calcium ATPase are the same with strontium and with calcium bound to the transport sites.
pubmed:affiliation
Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254-9110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.