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Glutamine synthetase was partly purified from Chlorella pyrenoidosa. This enzyme activity was stimulated by dithioerythritol and 2′-3′-dim ercaptopropanol (BAL). Full activation was obtained by thioredoxins isolated from the cyanobacterium Synechococcus 6301, from spinach and by heated Chlorella extract. The apparent K m  for the purified thioredoxin B from Synechococcus 6301 was determined to be 0.022 (22 × 10 -9  M), suggesting a specific role for thioredoxins in regulating glutamine synthetase activity in this alga.

A Thioredoxin Activated Glutamine Synthetase in Chlorella