title: gamma-Glutamyltransferase from Marthasterias glacialis: purification procedures and enzyme characterisation.
abstract: 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.
authors.forename: B P
authors.initials: BP
authors.lastname: Glynn
authors.forename: D B
authors.initials: DB
authors.lastname: Johnson
mesh_terms: D000818:Animals; D002417:Cattle; D002432:Cecum / Q000201:enzymology; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D008970:Molecular Weight; D013045:Species Specificity; D013215:Starfish / Q000201:enzymology*; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D005723:gamma-Glutamyltransferase