Chemical modification of L-asparaginase with a comb-shaped copolymer of polyethylene glycol derivative and maleic anhydride.
Biochem Biophys Res Commun
; 184(1): 144-8, 1992 Apr 15.
Article
en En
| MEDLINE
| ID: mdl-1567419
ABSTRACT
L-Asparaginase from Escherichia coli, an anti-tumor enzyme, was chemically modified with two types of maleic anhydride copolymers with a comb-shaped form, the one composed of polyoxyethylene allyl methyl diether with the molecular weight of 13,000 (activated PM13) and the other of polyoxyethylene 2-methyl-2-propenyl methyl diether with 100,000 (activated PM100). The modified asparaginases (PM13- and PM100-asparaginases) exhibited the complete loss of immunoreactivity towards anti-asparaginase serum. The enzymic activity of PM100-asparaginase without immunoreactivity was well retained by 85% of non-modified one, while that of PM13-asparaginase was retained 46%. These results were discussed in relation to the chemical structure of modifying reagents including chain shaped-polyethylene glycol derivatives.
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Banco de datos:
MEDLINE
Asunto principal:
Polietilenglicoles
/
Asparaginasa
/
Anhídridos Maleicos
Idioma:
En
Año:
1992
Tipo del documento:
Article