Glycosylation of Escherichia coli L-asparaginase.
Reductive coupling with sodium cyanoborhydride has been used with lactose and N-acetylneuraminyl lactose to prepare glycosylated Escherichia coli L-asparaginase. A substantial degree of modification can be achieved without significant loss of enzyme activity. The lactosylated enzyme shows increased thermal stability and resistance to proteolytic cleavage and is cleared more rapidly from the plasma of mice, compared to native asparaginase. The effect on clearance varies directly with the degree of lactosylation. Asparaginase modified with N-acetylneuraminyl lactose, in contrast, with approximately 13.6 mol of N-acetylneuraminyl lactose/mol of enzyme, is cleared more slowly, with a t 1/2 that is approximately twice that of the native enzyme.[1]References
- Glycosylation of Escherichia coli L-asparaginase. Marsh, J.W., Denis, J., Wriston, J.C. J. Biol. Chem. (1977) [Pubmed]
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