title: [Modification of L-asparaginase with colominic acid and the new characteristics of the modified enzyme].
abstract: The colominic acid was covalently coupled to L-asparaginase molecule by reductive amination. Depending on the molar ratios of colominic acid-asparaginase (30:1, 50:1 and 100:1), a modified enzyme molecule contained 4.7, 7.2 and 12 colominic acid molecule, they retained 58%, 56% and 33.2% of the initial asparaginase activity, respectively. In comparison with the native enzyme, modified enzyme had lower immunogenicity and antigenicity, longer half-life time (in vitro), more resistance ability to trypsin proteolysis, and similar Km value for L-asparagine.
authors.affiliation: Department of Enzymology, Institute of Microbiology, Chinese Academy of Sciences, Beijing.
authors.forename: Y D
authors.initials: YD
authors.lastname: Wang
authors.forename: L
authors.initials: L
authors.lastname: Guo
authors.forename: S J
authors.initials: SJ
authors.lastname: Qian
authors.forename: G Z
authors.initials: GZ
authors.lastname: Meng
authors.forename: S Z
authors.initials: SZ
authors.lastname: Zhang
mesh_terms: D001215:Asparaginase / Q000276:immunology / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D011134:Polysaccharides / Q000302:isolation & purification / Q000494:pharmacology*
chemical_list: D011134:Polysaccharides; C014420:colominic acid; D001215:Asparaginase