Linked Life Data

1898866

Source:http://linkedlifedata.com/resource/pubmed/id/1898866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-2-20
pubmed:abstractText
The interaction between domain AB and domains CD*EF of pike parvalbumin III has been studied by intrinsic fluorescence spectroscopy. In the presence of Ca2+ ions, parvalbumin fragment 38-108 containing two calcium binding sites interacts with the short peptide 1-37 with association constant 10(5.3 +/- 0.5) M-1. Removal of Ca2+ ions results in the disappearance of the interaction. The affinity of the complex of the two fragments for calcium is 50-times higher than the affinity of the isolated fragment 38-108, but slightly lower than that of the intact protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
1076
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Noncovalent complex between domain AB and domains CD*EF of parvalbumin.
pubmed:affiliation
Institute of Biological Physics, U.S.S.R. Academy of Sciences, Pushchino, Moscow region.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.