Abstract
The activity of Alanine aminopeptidase( AAP ) was measured in the urine of healthy and urinary tract cancer patients , the results showed higher activity of (AAP) in patients compared to healthy . AAP was Purified from the urine of healthy and patients with urinary tract cancer by dialysis and gel filtration (Sephadex G – 50) and two isoenzymes of (AAP) were separated from urine by using ion-exchang resin (DEAE – Sephadex A – 50 ) in previous study. The kinetics studies showed that both isoenzymes I and II obeyed Michaelis – Menton equation . with optimal concentration of alanine-4-nitroanilide as substrate for isoenzymes I and II which was (2 x 10-3 mol/L ). The two isoenzymes obeyed Arrhenius equation up two 37° C and their Ea and Q10 constants were determined . The binding of alanine-4-nitroanilide by two isoenzymes I , II were studied and the kinetic constant ( k+1 , k-1 , Ka , Ks ) were indicated that the reaction was first order at 37° C .Thermodynamic parameters of the standard state ( ∆G°,∆H° , ∆S° ) and the transition state ( ∆G*, ∆H* , ∆S* ) were determined by using Vant Hoff and Arrhenius equations.
Article Type
Article
How to Cite this Article
Al-Akabie, Taghreed U.
(2014)
"Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer,"
Baghdad Science Journal: Vol. 11:
Iss.
1, Article 9.
DOI: https://doi.org/10.21123/bsj.2014.11.1.70-80
