Linked Life Data

9273885

Source:http://linkedlifedata.com/resource/pubmed/id/9273885

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-1-8
pubmed:abstractText
Calcium binding studies of a 14-residue peptide corresponding to the 37-46 sequence of bovine factor X were performed using calcium ion selective electrode titrations and equilibrium dialysis. The presence of gamma-carboxyglutamic acid residues at positions 36 and 40 coupled with the assumption that the peptide would bind calcium ions also prompted an investigation of possibly secondary conformational changes in the peptide by use of circular dichroism spectroscopy. Equilibrium dialysis revealed a single relatively weak calcium binding site (log Ka = 2.39); an ion selective electrode experiment confirmed this result (log Ka = 2.17). The peptide maintained a random coil conformation throughout the calcium ion titrations as measured by circular dichroism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1397-002X
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Studies on the peptide corresponding to residues 34-47 of bovine factor X.
pubmed:affiliation
Department of Chemistry, University of North Carolina at Chapel Hill, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.