Local bacterial isolates (one hundred) were screened for production of alkaline protease (E.G.: 3.4.24.40) in solid and submerged cultures. The isolate Pseudomonas aeruginosa MS71 was selected based on its high production of enzyme and used in the present study. The optimum conditions for alkaline protease production were in VG (Van Gundy) medium, which consist of 1% glutamic acid, 0.2% sucrose and 0.5% casein with an initial pH8 after 72hrs of incubation at 35°C. Alkaline protease was purified from P. aeruginosa MS71 isolate by several steps including saturation of crude extract by ammonium sulphate (80%), ion exchange chromatography by DEAE-Celluose and gel filtration on sephadex G-75. The overall purification folds were 10.87 with 13.1% recovery. The characterization of the partial purified enzyme showed that its molecular weight was 38911 Dalton as determined by gel filtration. The enzyme activity was higher at neutral or basic pH and also it most stable at pH8. The maximum enzyme activity was observed at 35°C and it was stable at 60°C for 30 min, indicating that this enzyme is heat stable. The enzyme was highly specific towards, casein as a substrate. The average of the obtained values of Michaelis constant (km) and maximum velocity (Vmax) for alkaline protease were 0.575mM and Vmax was 451.56mM/min respectively. The effect of some ions inhibitors, reducing and chelating agents showed that Zn+2 and Ca+2 ions may play a role in the enhancement and stability of the enzyme, while activity was not inhibited in the presence, of reducing agent such as cysteine, 2-mercaptoethanol, dithiotheritol (DDT), but the enzyme activity was inhibited in the presence of EDTA with a .concentration l0mM indicating that the enzyme was a metalloprotease.