a product inhibition study on adenosine deminase dy spectroscopy and calorimetry

نویسنده:
,
سال
: 2002
چکیده: 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.
کلیدواژه(گان): adenosine deaminase- inosine product inhibition-constant- isothermal titration calorimetry
کالکشن :
  • نمایش متادیتا
  • آمار بازدید