Prikladnaia biokhimiia i mikrobiologiia · 2017
[PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications].
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Melik-Nubarov N S, Grozdova I D, Lomakina G Yu, Pokrovskaya M V, Pokrovski V S, Aleksandrova S S, Abakumova O Yu, Podobed O V, Grishin D V, Sokolov N N
Аннотация
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.
Предметные рубрики MeSH
Antineoplastic Agents, PhytogenicAsparaginaseBacterial ProteinsCell SurvivalChromatography, GelCloning, MolecularCross-Linking ReagentsEscherichia coliGene ExpressionHL-60 CellsHumansJurkat CellsK562 CellsPectobacterium carotovorumPolyethylene GlycolsProtein EngineeringRecombinant ProteinsSuccinimides