Linked Life Data

12767334

Source:http://linkedlifedata.com/resource/pubmed/id/12767334

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2003-5-27
pubmed:abstractText
Arsenate reductase (ArsC) from Staphylococcus aureus pI258 is extremely sensitive to oxidative inactivation. The presence of oxidized ArsC forms was not that critical for NMR, but kinetics and crystallization required an extra reversed-phase purification to increase sample homogeneity. The salt ions observed in the X-ray electron density of ArsC were investigated. Carbonate was found to have the lowest dissociation constant for activation (K(a)=1.1 mM) and potassium was stabilizing ArsC (DeltaT(m)=+6.2 degrees C). Also due to the use of these salt ions, the final yield of the purification had improved with a factor of four, i.e. 73 mg/l culture.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1570-0232
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
790
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
217-27
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Purification of an oxidation-sensitive enzyme, pI258 arsenate reductase from Staphylococcus aureus.
pubmed:affiliation
Dienst Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Vrije Universiteit Brussel, Paardenstraat 65, B-1640, Sint-Genesius-Rode, Belgium. jmessens@vub.ac.be
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't