gamma-Glutamyltransferase from Marthasterias glacialis: purification procedures and enzyme characterisation

gamma-Glutamyl transferase has been purified 239-fold from the pyloric caeca of Marthasterias glacialis. It has a mol. wt. of 229,000. The pH optima for the hydrolysis and transfer reactions are 5.0 and 9.2. Novel purification procedures using hydroxyhexyl and aminohexyl derivatives of Sepharose 4B are described. The enzyme was bound by immobilised m-aminophenylboronic acid but not by immobilized concanavalin A.