Y. Al-Abbasy, O., I. Al-Lehebe, N., A. Al-Bajari, S. (2014). Purification of Glutathion Peroxidase and Determination of it's Relation with some biochemical parameters in type II Diabetic patients. Alustath, 13(2), 1013-1030.
Omar Y. Al-Abbasy; Nashwan I. Al-Lehebe; Shihab A. Al-Bajari. "Purification of Glutathion Peroxidase and Determination of it's Relation with some biochemical parameters in type II Diabetic patients". Alustath, 13, 2, 2014, 1013-1030.
Y. Al-Abbasy, O., I. Al-Lehebe, N., A. Al-Bajari, S. (2014). 'Purification of Glutathion Peroxidase and Determination of it's Relation with some biochemical parameters in type II Diabetic patients', Alustath, 13(2), pp. 1013-1030.
Y. Al-Abbasy, O., I. Al-Lehebe, N., A. Al-Bajari, S. Purification of Glutathion Peroxidase and Determination of it's Relation with some biochemical parameters in type II Diabetic patients. Alustath, 2014; 13(2): 1013-1030.

Purification of Glutathion Peroxidase and Determination of it's Relation with some biochemical parameters in type II Diabetic patients

College Of Basic Education Research Journal
Article 38, Volume 13, Issue 2, December 2014, Pages 1013-1030    PDF (0 K)
Authors
Omar Y. Al-Abbasy; Nashwan I. Al-Lehebe; Shihab A. Al-Bajari
Abstract
The research includes the determination of Glutathione peroxidase activity and its relationship with some biochemical parameters in serum of patients of diabetes type II. The activity Glutathione peroxidase, Glutathione-s-transferase and the level of Glutathione are significantly decreased (p<0.05). whereas the activity of Superoxide dismutase, Polyamine oxidase and the levels of glucose, Glycocylated hemoglobin, Malondialdehyde, insulin hormone and insulin hormone resistance are increased significantly in patients compared to that of healthy subjects.
A positive correlation is found between Glutathione peroxidase with Glutathione-s-transferase (r=0.417), Superoxide dismutase (r=0.644) and Glutathione (r=0.521), whereas a significant negative correlation is found between Glutathione peroxidase with Malondialdehyde (r= -0.452).
The present study also deals with partial purification of Glutathione peroxidase from serum of Type II diabetic patients by dialysis, and ion exchange DEAE-cellulose techniques. One proteinous peak of Glutathione peroxidase activity is obtained with specific activity of 0.128 Umg protein and purification fold 10.27 compared to crude enzyme.
The kinetic characteristics of partially purified Glutathione peroxidase are studied. The maximum activity is obtained at 12.8µg of enzyme, Na-K phosphate buffer solution at pH 7.3, temperature 37C, incubation time 8 min., with 10 mM Na+1 . Vmax and Km values of partially purified Glutathione peroxidase with the substrate, Glutathione are found 0.31unit/ml and 1.538 mM respectively.
Keywords
Purification; Glutathion; peroxidase
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