IMMUNOLOGICAL STUDIES OF AN EXTRACELLULAR KERATINASE

Abstract

ABSTRACT The extracellular keratinase from M. canis was purified using ion exchange chromatography and gel filtration. The purified enzyme showed a single protein band on sodium dodecyl sulfate‐polyacrilamide gel electrophoresis. A molecular weight of approximately 45,000 was determined by SDS‐electrophoresis. Anti‐body directed against the purified enzyme from M. canis was obtained from New Zealand White rabbits, and the immunological identity of the enzyme from M. canis , as well as those from M. gypseum, T. mentagrophytes and T. rubrum , were demonstrated by immuno‐double‐diffusion experiments.