Purification, modification, physico-chemical and pharmacokinetic characterization of arginase, an enzyme of potential use in therapy
Visco, C.; Benassi, C.A.; Veronese, F.M.; Miglioli, P.A.
Il Farmaco; Edizione Scientifica 42(8): 549-559
1987
ISSN/ISBN: 0430-0920 PMID: 3117587 Document Number: 300583
Beef liver arginase, an enzyme potentially useful in the therapy of arginine dependent tumors or of familial hydroargininemia, was purified to homogeneity by a procedure involving a key step of hydrophobic affinity chromatography. The enzyme was extensively modified by the covalent linking of monomethoxypolyethyleneglycol molecules according to a procedure recently proposed by the Authors (Veronese et al., Appl. Biochem. Biotecnol. 11, 869, 1985) without any significant loss of activity. The derivative enzyme presents more convenient properties for a therapeutic use, as compared to the native enzyme, such an increased structural stability, a decreased digestion by proteolytic enzymes and an expanded clearance time in rats.