Abstract
γ-Glutamyl transferase from the pyloric caeca of Marthasterias glacialis has been purified to apparent homogeneity. 1. 2. The enzyme consists of four subunits, each of approx, mol. wt. 60,000. 2. 3. The enzyme was inactivated by photooxidation in the presence of Rose Bengal, by a carbodiimide derivative and by N- acetylimidazole . 3. 4. Inactivation by N- acetylimidazole , which eliminated the activation of the enzyme by Gly-Gly, was never more than 50%. It is concluded that this acetylating reagent modifies part of the aminoacylglycine binding site.
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