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 |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Bioconjugation Chromatography biology Polyethylene glycol Erwinia biology.organism_classification Applied Microbiology and Biotechnology Biochemistry law.invention Sepharose 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Tetramer law Reagent PEG ratio Recombinant DNA |
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 |
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