Identification of myeloperoxidase in human colostrum.

The properties of a peroxidase in human colostrum were studied using antiserum against human myeloperoxidase. The peroxidase in human colostrum gave a single precipitin line against the antiserum on double immunodiffusion, and this precipitin line fused completely with the precipitin line formed between myeloperoxidase and the antiserum. The peroxidase activity in human colostrum was precipitated completely with anti-myeloperoxidase IgG, like myeloperoxidase activity. The peroxidase of colostral whey was purified to homogeneity. The purified enzyme consisted of two subunits of Mr 59,000 and 15,000, corresponding in size to the two subunits of myeloperoxidase. Immunostaining of a protein blot from a sodium dodecyl sulfate-polyacrylamide electrophoresis gel also showed that the peroxidase in the whey extract consisted of the same two subunits as myeloperoxidase. These results indicate that the peroxidase of human colostrum is identical with myeloperoxidase.