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Glutamine synthetase (EC 6.3.1.2] has been purified from the green alga Monoraphidium braunii. The enzyme was purified by a method which included consecutive chromatographies on: DEAE Sepharose, Blue Sepharose, second DEAE Sepharose, Sephacryl S-300 and Phenyl Sepharose CL-4B. The apparent molecular weight of the GS subunit was approximately 42 000. Since the undissociated enzyme has a molecular...
Monoraphidium braunii glutamine synthetase is inactivated by several mixed-function oxidation systems. Inactivation requires oxygen and a metal cation as it does not take place under anaerobic conditions or in the presence of EDTA. Glutamine synthetase can be protected against that inactivation by peroxidase and catalase but not by superoxide dismutase indicating that hydrogen peroxide is involved...
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