Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2007-1-26
pubmed:abstractText
Thermal denaturation of Euphorbia latex amine oxidase (ELAO) has been studied by enzymatic activity, circular dichroism and differential scanning calorimetry. Thermal denaturation of ELAO is shown to be an irreversible process. Checking the validity of two-state it really describes satisfactorily the thermal denaturation of ELAO. Based on this model we obtain the activation energy, parameter T(*) (the absolute temperature at which the rate constant of denaturation is equal to 1 min(-1)), and total enthalpy of ELAO denaturation. HPLC experiments show that the thermal denatured enzyme conserves its dimeric state. The N(2)-->kD(2) model for thermal denaturation of ELAO is proposed: where N(2) and D(2) are the native and denatured dimer, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
254-9
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Two-state irreversible thermal denaturation of Euphorbia characias latex amine oxidase.
pubmed:affiliation
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't