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  • Title: [PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications].
    Author: Melik-Nubarov NS, Grozdova ID, Lomakina GY, Pokrovskaya MV, Pokrovski VS, Aleksandrova SS, Abakumova OY, Podobed OV, Grishin DV, Sokolov NN.
    Journal: Prikl Biokhim Mikrobiol; 2017; 53(2):164-72. PubMed ID: 29508977.
    Abstract:
    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.
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