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OJVRTM
Online Journal of Veterinary Research©
Volume 21(7):410-427, 2017.
Method to
conjugate L-Aspariginase with Carboxymethyl
Dextran
Marjan Chahardahcherik, Mahboobeh Ashrafi, Mahmoud Aminlari*
aDepartment of Biochemistry,
School of Veterinary Medicine, Shiraz University, Shiraz, 71345 Iran *Mahmoud Aminlari, E. mail: aminlari@shirazu.ac.ir.
ABSTRACT
Chahardahcherika M, Ashrafia M, Aminlaria M., Method
to conjugate L-Aspariginase with Carboxymethyl
Dextran, Onl J Vet Res., 21(7):410-427, 2017. L-asparaginase aminohydrolase is used to manage childhood acute leukemia
and non-Hodgkin's lymphoma by catalyzing hydrolysis of asparagine to aspartic
acid and ammonia. The enzyme also
prevents formation of acrylamide in foods processed at high temperatures. A
method to conjugate L-asparaginase with carboxymethyl dextran (CMD) to increase specific activity
is described. Conjugation was performed at pH 7.2 or 8.5 at
a CMD:asparaginase molar
ratio of 85:1 for 2h at room temperature. Conjugation was determined by presence of free amino groups and SDS-PAGE.
Findings suggested that conjugation with
CMD increased specific activity of L-asparaginase 2-3 fold, and its Michaelis constant (Km) 2-7 fold.
Key words: L-asparaginase,
conjugation, carboxymethyl dextran, enzyme activity,
kinetic properties.
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