Abstract
This study was aimed to purify, characteristic, and fibrinolytic activity of staphylokinase (SAK), is an enzyme activates plasminogen to form plasmin, which digest fibrin clots that cause thrombosis clot. Staphylokinase was purified from local isolate Staphylococcus aureus GH38 by ammonium sulfate precipitation at 70% saturation followed by ion exchange chromatography (CM-Cellulose) with a purification fold 2.73, and 1.53, and recovery 72.1, and 33.11% in wash and elution steps respectively. The partially purified enzyme was high activity at 40°C with pH 7 and the enzyme retained 100% of its activity at 35°C with pH 7. The activity of an enzyme increased by its treatment with calcium and sodium chloride, while the activity affected when incubated with mercury, silver, and iron chloride. The enzyme have high effective against thrombus (blood clot), which encourage the use of enzyme in the treatment as therapeutic agent to remove clots formed in the human body.
Highlights
33.11% in wash and elution steps respectively
This study was aimed to partial purification and characterization of staphylokinase from locally isolate of Staphylococcus aureus GH38 as well as therapeutic agent to remove blood clots [14]
GH38 was partially purified with ammonium coccus aureus VITSDVM7 was precipitated sulfate precipitation its considered as an im- with 75 % (NH4)2So4 and showed maximum portant methods for purification of enzymes level of enzyme activity on which specific ac
Summary
33.11% in wash and elution steps respectively. The partially purified enzyme was high activity at 40°C with pH 7 and the enzyme retained 100% of its activity at 35°C with pH 7. This study was aimed to partial purification and characterization of staphylokinase from locally isolate of Staphylococcus aureus GH38 as well as therapeutic agent to remove blood clots [14].
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