PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications

Autor: G. Yu. Lomakina, S. S. Aleksandrova, O. V. Podobed, D. V. Grishin, N. S. Melik-Nubarov, I. D. Grozdova, O. Yu. Abakumova, M. V. Pokrovskaya, Nikolay N. Sokolov, V. S. Pokrovski
Rok vydání: 2017
Předmět:
Zdroj: Applied Biochemistry and Microbiology. 53:165-172
ISSN: 1608-3024
0003-6838
Popis: N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from Erwinia carotovora. A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed. The best results were produced by modification of the enzyme with a 25-fold excess of reagent relative to the enzyme tetramer. The modified L-asparaginase was isolated from the reaction mixture by gel filtration on Sepharose CL-6B. The purified bioconjugate did not contain PEG unbound to the protein, demonstrated high catalytic activity, and exhibited antiproliferative action on cell cultures.
Databáze: OpenAIRE