Abstract
(1) Lactoperoxidase-goat antihuman IgG and alkaline phosphatase-goat antihuman IgG mixtures were coupled with glutaraldehyde, and the mixtures fractionated by gel chromatography and sucrose density gradients. Less glutaraldehyde was required to polymerize goat IgG and lactoperoxidase than was required to polymerize alkaline phosphatase. Goat IgG and lactoperoxidase polymerized as globular aggregates, while alkaline phosphatase polymerized as extended chains. (2) Increasing the glutaraldehyde concentration used to conjugate alkaline phosphatase to goat IgG increased the loss of both antibody activity and enzyme activity. However, the enzyme activity bound to the active antibody did not change with increasing glutaraldehyde concentration. (3) A low glutaraldehyde concentration coupled 49% of the lactoperoxidase to functional antibody. This conjugate was useful for localizing human IgG deposits in tissue for light microscopy. Because a low concentration of glutaraldehyde efficiently coupled lactoperoxidase to antibody, lactoperoxidase may prove to be a useful substitute for horseradish peroxidase.
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