A kinetic study of the reaction between glutaraldehyde and horseradish peroxidase.
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.
D000447:Aldehydes / Q000378:metabolism*; D005976:Glutaral / Q000378:metabolism*; D006651:Histocytochemistry; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010544:Peroxidases / Q000378:metabolism*; D013696:Temperature
D000447:Aldehydes; D006735:Horseradish Peroxidase; D010544:Peroxidases; D005976:Glutaral