Linked Life Data

18769736

Source:http://linkedlifedata.com/resource/pubmed/id/18769736

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-10-15
pubmed:abstractText
A reversible effect of pH on the ionization of amino-acid residues at the active center of choline oxidase was observed near the optimum pH (8). Inactivation of choline oxidase took place in the pH ranges 3-6 and 9-11, in which irreversible changes in the structure occur leading to the enzyme inactivation. The first order rate constants of the enzyme's inactivation at various pH values were estimated for the irreversible changes. The Arrhenius analysis revealed no significant changes in the activation enthalpy, while an increase in the activation entropy reflected an increase in the conformational freedom.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-527X
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
549-57
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Effects of pH on the activity and structure of choline oxidase from Alcaligenes species.
pubmed:affiliation
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't