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Chemistry of Natural Compounds

, Volume 22, Issue 6, pp 712–717 | Cite as

Immobilization of the enzyme L-asparaginase fromE. coli on polysaccharides IV. Covalent binding with dialdehyde-dextran

  • A. S. Karsakevich
  • S. N. Shulichenko
  • M. R. Buka
  • I. A. Vina
  • A. P. Kashkin
Article

Abstract

The synthesis has been effected of immobilizedE. coli L-asparaginase on medical dextran — poliglyukin. The influence of the bound polymer on some physicochemical properties of the final products have been studied. An increased resistance to heat and stability on storage of the immobilized forms of L-asparagine in comparison with a native enzyme has been found. It has been shown that the polymer modification of L-asparaginase leads to a decrease in the antigenic affinity of the immobilized enzyme as compared with the native enzyme.

Keywords

Native Enzyme Asparaginase Cyanogen Bromide Polymer Conjugate Immobilize Form 

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Copyright information

© Plenum Publishing Corporation 1987

Authors and Affiliations

  • A. S. Karsakevich
  • S. N. Shulichenko
  • M. R. Buka
  • I. A. Vina
  • A. P. Kashkin

There are no affiliations available

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