a product inhibition study on adenosine deminase dy spectroscopy and calorimetry
Year
: 2002
Abstract: 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 27oC 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 µM by the microcalorimetry method, which
agrees well with the value of 143 µM for the inhibition
constant that was obtained from the spectroscopy method.
the effect of the inosine product on the activity of
adenosine deaminase in a 50 mM sodium phosphate
buffer, pH 7.5, at 27oC 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 µM by the microcalorimetry method, which
agrees well with the value of 143 µM for the inhibition
constant that was obtained from the spectroscopy method.
Keyword(s): adenosine deaminase- inosine product inhibition-constant- isothermal titration calorimetry
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a product inhibition study on adenosine deminase dy spectroscopy and calorimetry
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| contributor author | محمدرضا حسین دخت | en |
| contributor author | Mohammad Reza Housaindokht | fa |
| date accessioned | 2020-06-06T14:35:46Z | |
| date available | 2020-06-06T14:35:46Z | |
| date issued | 2002 | |
| identifier uri | http://libsearch.um.ac.ir:80/fum/handle/fum/3403318?locale-attribute=en | |
| description abstract | 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 27oC 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 µM by the microcalorimetry method, which agrees well with the value of 143 µM for the inhibition constant that was obtained from the spectroscopy method. | en |
| language | English | |
| title | a product inhibition study on adenosine deminase dy spectroscopy and calorimetry | en |
| type | Journal Paper | |
| contenttype | External Fulltext | |
| subject keywords | adenosine deaminase- inosine product inhibition-constant- isothermal titration calorimetry | en |
| journal title | journal of biochemistry and molecular biology | en |
| journal title | Journal of Biochemistry and Molecular Biology | fa |
| pages | 302-305 | |
| journal volume | 35 | |
| journal issue | 3 | |
| identifier link | https://profdoc.um.ac.ir/paper-abstract-201088.html | |
| identifier articleid | 201088 |