Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer
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...
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| Format: | Article |
| Language: | Arabic |
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College of Science for Women, University of Baghdad
2014-03-01
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| Series: | Baghdad Science Journal |
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| Online Access: | http://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/1535 |
| _version_ | 1818369054603214848 |
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| author | Baghdad Science Journal |
| author_facet | Baghdad Science Journal |
| author_sort | Baghdad Science Journal |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-13T23:17:45Z |
| format | Article |
| id | doaj.art-5a8714dd5acb42af9e39514b30fbced2 |
| institution | Directory Open Access Journal |
| issn | 2078-8665 2411-7986 |
| language | Arabic |
| last_indexed | 2024-12-13T23:17:45Z |
| publishDate | 2014-03-01 |
| publisher | College of Science for Women, University of Baghdad |
| record_format | Article |
| series | Baghdad Science Journal |
| spelling | doaj.art-5a8714dd5acb42af9e39514b30fbced22022-12-21T23:27:53ZaraCollege of Science for Women, University of BaghdadBaghdad Science Journal2078-86652411-79862014-03-0111110.21123/bsj.11.1.70-80Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract CancerBaghdad Science JournalThe 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.http://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/1535 |
| spellingShingle | Baghdad Science Journal Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer Baghdad Science Journal |
| title | Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer |
| title_full | Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer |
| title_fullStr | Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer |
| title_full_unstemmed | Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer |
| title_short | Kinetic and thermodynamic Studies Of Alanine Aminopeptidase(AAP) Isoenzymes I,II Partially Purified From Patient's Urine With Urinary Tract Cancer |
| title_sort | kinetic and thermodynamic studies of alanine aminopeptidase aap isoenzymes i ii partially purified from patient s urine with urinary tract cancer |
| topic | |
| url | http://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/1535 |
| work_keys_str_mv | AT baghdadsciencejournal kineticandthermodynamicstudiesofalanineaminopeptidaseaapisoenzymesiiipartiallypurifiedfrompatientsurinewithurinarytractcancer |