Study the characteristics of partially purified arginase from the serum of patients with diabetes mellitus type two (DMT2) in the Nineveh Governorate

Abstract

Arginase plays an essential role in diabetes mellitus type 2 (DMT2). The study aimed to isolate and partially purify the serum arginase from patients with diabetes mellitus type 2, estimate its molecular weight, and determine the optimal conditions for the enzyme's action. The study included 35 patients of both sexes of 16 males and 19 females. Three purification steps were used to purify arginase are the precipitation of the protein with ammonium sulfate at a saturation of 65%, DEAE-cellulose ion-exchange chromatography, and Sephadex G-100 gel scattering technique. The results showed that the specific activity of unpurified arginine is equal to 0.6 and the specific activity increased 19 times when purified while the specific activity was equal to 11.4 (U/mg). The number of purification times was 19-fold, and recovery of 59.2 %. And the molecular weight of purified arginase equals 96050 ± 1414.2 Daltons. The highest activity of purified arginase in 250 µL serum as a source of enzyme,100 mM of buffer solution sodium barbitone, pH = 9.5, and time incubation for 45 minutes at 37 C, and 200 mM of arginine as a substrate for arginase. The study concluded that the specific activity of arginase from serum of diabetic patients increased 19 times after purification. The properties of arginine and the optimal conditions for its action are differ according to the source of the enzyme purified that from it.