Linked Life Data

12297022

Source:http://linkedlifedata.com/resource/pubmed/id/12297022

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-9-25
pubmed:abstractText
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at 27 degrees C using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 140 microM by the microcalorimetry method, which agrees well with the value of 143 microM for the inhibition constant that was obtained from the spectroscopy method
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1225-8687
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
302-5
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
A product inhibition study on adenosine deaminase by spectroscopy and calorimetry.
pubmed:affiliation
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. saboury@chamran.ut.ac.ir
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't