Protease in polyhedral protein is precipitated with 0.1 saturation of ammonum sulphate but that in silkworm tissue with 0.2-0.5 saturation. The both proteolytic enzymes display the highest activity at pH 10.5 ; they are destroyed by heating at 70 ℃ for 10 minutes. The protease of polyhedral protein is inhibited by copper sulphate of high normality, chloramphenicol palmitate, chloramphenicol, p-chloromercuribenzoic acid, flavin adenine dinucleotide, 8-azaguanine, nitrogen mustard, aureomycin or potato inhibitor, and activated by copper sulphate of low concentration, urea, thiourea, cysteine or ascorbic acid. The proteolytic action, however, is not influenced by theophylline, uric acid, calcium oxalate, calcium chloride, magnesium sulphate, sodium azide, hydrogen peroxide, ethylendiamine tetraacetic acid, monoiodoacetic acid, potassium cyanide, adenosine triphosphate, 8-azaxanthine, nitromin, mitomycin, carzinophilin and 6-mercaptophyrin.
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