PEGylated recombinant L-asparaginase from <Emphasis Type="Italic">Erwinia carotovora</Emphasis>: Production,properties, and potential applications |
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Authors: | N S Melik-Nubarov I D Grozdova G Yu Lomakina M V Pokrovskaya V S Pokrovski S S Aleksandrova O Yu Abakumova O V Podobed D V Grishin N N Sokolov |
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Institution: | 1.Department of Chemistry,Lomonosov Moscow State University,Moscow,Russia;2.Orekhovich Scientific Research Institute of Biomedical Chemistry,Moscow,Russia |
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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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