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PROTAMINE PURIFICATION OF STREPTOKINASE AND EFFECT OF pH AND TEMPERATURE ON REVERSIBLE INACTIVATION.

L R Christensen¹

¹Department of Bacteriology, New York University College of Medicine, New York.

The Journal of General Physiology

|October 30, 2009

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Protamine treatment purifies streptokinase by removing impurities without losing activity. Streptokinase stability depends on pH and temperature, with reversible inactivation at pH 5 and irreversible inactivation above 23°C or pH 9.

Area of Science:

Biochemistry
Protein Chemistry
Enzymology

Background:

Streptokinase is a crucial thrombolytic agent.
Crude streptokinase preparations contain impurities like nucleic acids and protease inhibitors.
Understanding streptokinase stability is vital for its therapeutic application.

Purpose of the Study:

To investigate the purification of streptokinase using protamine.
To characterize the stability of streptokinase solutions concerning pH and temperature.

Main Methods:

Treatment of crude streptokinase concentrates with protamine.
Assessing the impact of pH and temperature on streptokinase activity and stability.
Monitoring nitrogenous material removal during purification.

Keywords:

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Main Results:

Protamine treatment effectively removed approximately 90% of nitrogenous impurities, including nucleic acid and protease inhibitor, with minimal loss of streptokinase activity.
Streptokinase solutions exhibited reversible inactivation, particularly around pH 5.
Both inactivation and reactivation rates were influenced by pH and temperature, with irreversible inactivation occurring above 23°C or pH 9.

Conclusions:

Protamine is an effective agent for purifying streptokinase, enhancing its therapeutic potential.
Streptokinase exhibits distinct pH and temperature-dependent stability profiles, crucial for formulation and administration.
Optimal conditions for streptokinase handling and storage can be defined based on its inactivation kinetics.