Linked Life Data

11710019

Source:http://linkedlifedata.com/resource/pubmed/id/11710019

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-11-16
pubmed:abstractText
The thermoinactivation of native diisopropylfluorophosphatase (DFPase, EC 3.8.2.1) is highly calcium dependent, first-order kinetic. Deactivation is coupled with a simultaneous reduction in beta-sheet content. We report herein our attempts to enhance the thermostability of DFPase by irreversibly incorporating the enzyme into polyurethane polymers. Immobilized DFPase has biphasic deactivation kinetics. Our data demonstrate that the initial rapid deactivationof immobilized DFPase leads to the formation of a hyperstable and still active form of enzyme. Like native DFPase, DFPase-containing polyurethanes exhibit a calcium-dependent thermostability. Since bioplastics cannot be analyzed by spectroscopy, the structural mechanisms involved in thermoinactivation of immobilized DFPase were determined using PEG-modified DFPase. The thermoinactivation profile of highly modified DFPase mirrors the stepwise deactivation pattern of bioplastics. Spectroscopic studies enable a structural analysis of the hyperstable intermediate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1525-7797
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
664-71
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Thermoinactivation of diisopropylfluorophosphatase-containing polyurethane polymers.
pubmed:affiliation
Department of Chemical and Petroleum Engineering & Center for Biotechnology and Bioengineering, University of Pittsburgh, 1249 Benedum Hall, Pittsburgh, Pennsylvania 15261, USA.
pubmed:publicationType
Journal Article, In Vitro