A procedure was developed for simultaneous isolation of aspartyl and cysteine proteinases as well as of the cysteine-proteinase inhibitors. Affinity chromatography using pepstatin-Sepharose enabled one to isolate aspartyl proteinases, while inhibitors of cysteine-proteinases were isolated by affinity chromatography on CM-papain-Sepharose; further purification of the enzymes was carried out using ion exchange chromatography and gel filtration. Partially purified preparations of cathepsin D as well as of cysteine-proteinases and their inhibitors were obtained. Some physicochemical and enzymatic properties of the enzymes and inhibitors obtained were studied.

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