Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer Taghreed U.Al-Akabie

Main Article Content

Baghdad Science Journal

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.

Downloads

Download data is not yet available.

Article Details

How to Cite
1.
Journal BS. Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient’s Urine With Urinary Tract Cancer. BSJ [Internet]. 2Mar.2014 [cited 24Aug.2019];11(1):70-. Available from: http://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/1535
Section
article

Most read articles by the same author(s)

1 2 3 4 5 6 7 8 9 10 > >>