Linked Life Data

9713705

Source:http://linkedlifedata.com/resource/pubmed/id/9713705

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-10-19
pubmed:abstractText
Some properties of catalase and horseradish peroxidase entrapped into reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate (AOT)/n-heptane with those in an aqueous solution of AOT are compared. Secondary structure of catalase significantly changes and activity is completely lost in the presence of aqueous micellar solution of AOT. In AOT/n-heptane reverse micelles secondary structure of catalase does not change. AOT has no effect on horseradish peroxidase in aqueous solution. On the other hand slight changes in secondary structure of horseradish peroxidase in AOT/n-heptane reverse micelles appear. It is concluded that electrostatic interactions between catalase or horseradish peroxidase with AOT molecule at neutral pH are not the main factor determining reactivity of investigated enzymes in reverse micelles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
805-11
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Interaction of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) with catalase and horseradish peroxidase in an aqueous solution and in the reverse micelles of AOT/N-heptane.
pubmed:affiliation
Institute of Applied Radiation Chemistry, Technical University of Lód?, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't