title: Purification and properties of L-glutaminase-L-asparaginase from Pseudomonas acidovorans.
abstract: An enzyme that catalyzes the hydrolysis of both glutamine and asparagine has been purified to homogeneity from extracts of Pseudomonas acidovorans. The enzyme having a ratio of glutaminase to asparaginase of 1.45:1.0 can be purified by a relatively simple procedure and is stable upon storage. The glutaminase-asparaginase has a relatively high affinity for L-asparagine (Km=1.5 X 10(-5) M) and L-glutamine (Km=2.2 X 10(-5) M) and has a molecular weight of approximately 156,000 the subunit molecular weight being approximately 39,000. Injections of the enzyme produced only slight increases in the survival time of C3H/HE mice carrying the asparagine-requiring 6C2HED Gardner lymphoma and of white Swiss mice carrying the glutamine-requiring Ehrlich lymphoma.
mesh_terms: D000581:Amidohydrolases / Q000302:isolation & purification; D000818:Animals; D001215:Asparaginase / Q000302:isolation & purification / Q000378:metabolism / Q000627:therapeutic use; D005972:Glutaminase / Q000302:isolation & purification / Q000378:metabolism / Q000627:therapeutic use; D007700:Kinetics; D051379:Mice; D008809:Mice, Inbred C3H; D008970:Molecular Weight; D009374:Neoplasms, Experimental / Q000188:drug therapy; D011549:Pseudomonas / Q000201:enzymology*
chemical_list: D000581:Amidohydrolases; D001215:Asparaginase; D005972:Glutaminase; C020654:glutamin-(asparagin-)ase