title: Purification, modification, physico-chemical and pharmacokinetic characterization of arginase, an enzyme of potential use in therapy.
abstract: Beef liver arginase, an enzyme potentially useful in the therapy of arginine dependent tumors or of familial hyperargininemia, 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.
mesh_terms: D000818:Animals; D001119:Arginase / Q000302:isolation & purification* / Q000378:metabolism / Q000627:therapeutic use; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D004492:Edetic Acid; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D010447:Peptide Hydrolases; D011092:Polyethylene Glycols; D051381:Rats; D011919:Rats, Inbred Strains; D013696:Temperature
chemical_list: D011092:Polyethylene Glycols; D004492:Edetic Acid; D010447:Peptide Hydrolases; D001119:Arginase