Purification of Polyamine Oxidase from Diabetic Type-I Females and Studies of the Inhibitory Effect of some Thiourea Compounds on its Activity
Rafidain Journal of Science,
2014, Volume 25, Issue 2, Pages 105-122
AbstractThe research included a determination of polyamine oxidase (PAO) activity in normal females and diabetic type I patients. It was found that the activities of PAO in red blood cells (RBC) and plasma in patients were significantly higher than that of normal (p<0.05).
The partial purification of PAO from RBC of diabetic and normal females were included in this study. This was achieved by using different biochemical techniques. Three proteinous peaks with PAO activities in RBC (I, II, III) from each of normal, diabetic with specific activities (Umg protein) (0.194,0.183 and 0.098), (0.349, 0.237 and 0.176) were isolated from ion exchange chromatography. Molecular weights (72588, 74512 and 69339), (141458, 100671 and 104018) Da respectively.
This study didn't show the existence of Cu2+ ion as a cofactor for any PAO isoenzyme, but indicated the existence of flavin adenine dinucleotide(FAD) as a cofactor for all PAO isoenzymes.
On the other hand, the research included a preparation of thiourea derivatives of structure analogous to sulfonylurea drugs and containing thiosemicarbazide. Thiosemicarbazide showed an inhibitory effect on partially purified PAO activity. The prepared thiourea derivatives of thiosemicarbazide showed a competitive inhibition of PAO activity.
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