Study of the properties and inhibition of the polyamine oxidase enzyme partially purified from the fruit of green pepper by amyloride and medovi

• Main Authors: Wathba Touhala (Author), Muheeb Jassim (Author)
• Format: Book
• Published: College of Education for Pure Sciences, 2013-12-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Summary

<strong>ABSTRACT</strong><br /> The study included a detection of PAO in green pepper (<em>Capsicum grossum</em>) and its partial purification by using dialysis and anion exchange chromatography (using DEAE - cellulose) techniques . Two isoenzymes were obtained, with a specific activity of 3.9 and 2.6 unit / mg protein, and a purification fold of 21.4 and 14.3 respectively compared to crude enzyme. Copper ion in both isoenzymes was detected and found to be 0.1915 and 0.2947 mg / ml respectively.<br /> The maximum PAOI,II isoenzyme activity were obtained at 100 microlitre of enzyme, sodium phosphate buffer at pH 8.6,7.2, temperature at 40, 37°C, and 125 , 100 mM of spermidine as substrate respectively, and have a high specificity toward the polyamine, spermidine compared with other amine compounds.<br />      The inhibitory effect of the drugs amiloride and medovire on PAOI activity was studied and showed that increasing of inhibitor concentration led to a decrease in activity. The inhibition type was found to be competitive , and Ki were 0.88 and 1.1 mM respectively.<br />           Spermine was detected by HPLC technique from non-proteinous extract. Basic amino acids were  isolated by using  Amberlite 120 H⁺and Amberlite 50NH₄⁺ successively, the results indicated that the green pepper contained 96.1  mg / g of plant.

Item Description

1812-125X
2664-2530
10.33899/edusj.2013.163101