A kinetic study of the reaction between glutaraldehyde and horseradish peroxidaseSO Molin, H Nygren, L Dolonius and HA Hansson
Horseradish peroxidase was reacted with glutaraldehyde under various reaction conditions. The reaction product was, in a second step, bound covalently to aminohexyl groups attached to Sepharose particles. The influence of pH, time and the concentration ratio of enzyme:glutaraldehyde on the reaction was evaluated. A first step reaction with 100-fold molar excess of glutaraldehyde to horseradish peroxidase at pH 9.5 for 2 hr at room temperature results in a high yield of conjugated enzyme with well preserved enzymatic activity.
Volume 26,
Issue 12,
pp. 1053-1056,
12/01/1978
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