Abstract
A pepstatin insensitive protease was purified from mackerel white muscle by a combination of acid treatment, ammonium sulfate fraction, Q Sepharose Fast Flow ion exchange chromato-graphy, Cellulofine GC-200 gel filtration, hydrophobic chromatography on Phenyl-Superose column, chromatofocusing on Mono P column, re-chromatofocusing on the column, and ion ex-change chromatography on Mono Q column. The specific activity of the enzyme increased about 7, 750-fold in 1.6% yield, and the final preparation proved to be homogeneous on polyacryl-amide slab gel electrophoresis.
