Linked Life Data

15036286

Source:http://linkedlifedata.com/resource/pubmed/id/15036286

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2004-3-23
pubmed:abstractText
In this work we show, by a combination of biochemical and biophysical approaches, that the copper ions bound in the binuclear active site of Carcinus aestuarii hemocyanin play a stabilizing role on the tertiary structure of the protein. Upon removal of copper, the monomeric hemocyanin, but not the hexameric oligomer, undergoes changes at the level of tertiary structure while the secondary structure is almost unaffected. By Small-Angle X-Ray Scattering, supported by gel chromatography measurements, it can be concluded that the apo-monomer, but not the holo form or the hexameric form, undergoes a slow time-dependent oligomerization process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0968-4328
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-4
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Structural role of the copper ions in the dinuclear active site of Carcinus aestuarii hemocyanin.
pubmed:affiliation
Department of Biology, University of Padova, Via Ugo Bassi 58/B, Padova 35131, Italy.
pubmed:publicationType
Journal Article