Abstract
Rat liver peroxisomal catalase was purified to homogeneity. The starting material was purified peroxisomes, The purity of the final preparation was judged by Sephadex G-200 chromatography, SDS gel electrophoresis, spectral analysis, and immunochemical means. Two sera containing anticatalase antibodies were prepared. The first, a rabbit serum, contained a minor impurity. The anticatalase was purified forty times by affinity chromatography and the contaminating antibodies were thereby removed. The second serum, prepared in a goat, was proved to be monospecific by immunodiffusion and immunoelectrophoresis.