Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-11-25
pubmed:abstractText
The kinetic theory of the substrate reaction during modification of enzyme activity has been applied to study the inactivation kinetics of enzymes by denaturant. However, an important problem related to the determination of the inactivation rate constants has not been considered in a previous publication (Xiao, et al., Biochim. Biophys. Acta, 1164 (1993) 54-60). In most denaturation experiments, the high concentrations of denaturants may greatly affect the kinetic behavior of the system to preclude the use of the kinetic parameters determined in the absence of denaturant. In the present study, the kinetic equation of substrate reaction in presence of denaturant has been derived. A re-examination of the effect of high concentrations of guanidine hydrochloride on the inactivation of papain, taking into consideration the effect of high concentrations of guanidine hydrochloride on the Michaelis constant, showed that, for papain, the substrate gives no protection on its inactivation. It is the purpose of the present communication to stress the importance of observing the effect of the denaturant on the kinetic parameters for kinetic analysis of enzyme inactivation by denaturants generally.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
1388
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
The inactivation kinetics of papain by guanidine hydrochloride: a re-analysis.
pubmed:affiliation
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't