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In order to clarify the reason for the variation in specific activities of ribonuclease preparations from Rhizopus sp. ribonuclease (RNase Rh), low specific activity species (RNase Rh') were separated from native RNase Rh by DEAE Toyopearl 650 column chromatography and characterized. When RNase Rh' was subjected to gel electrophoresis in the absence of 2mercaptoethanol, it gave a 24 kilodalton (kDa) protein band, but in the presence of the reducing agent it gave 17 and 7 kDa bands. These twodoi:10.1248/cpb.35.4953 fatcat:ggeokpx3inffrpghojbhaxtesu