Linked Life Data

497250

Source:http://linkedlifedata.com/resource/pubmed/id/497250

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1980-1-19
pubmed:abstractText
The conformation of perch parvalbumin in the Ca-, Mg- and metal-free state was studied by intrinsic fluorescence, trypsin susceptibility, thiol titration and circular dichroism. The data reveal that Ca-parvalbumin has a more compact structure than the metal-free protein, with a high alpha-helical content and a buried thiol. No difference in conformation could be detected between Mg- and Ca-parvalvumin, indicating that the Ca-Mg exchange that may take place during muscular activity is accompanied by little or no structural changes. Furthermore, recently published kinetic parameters can now be interpreted as meaning that, during the contraction-relaxation cycle, parvalbumin often stays in the Mg-form instead of switching to the Ca-form which is predominant in vitro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
601-5
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Calcium, magnesium and the conformation of parvalbumin during muscular activity.
pubmed:publicationType
Journal Article