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- W2034006508 abstract "Abstract 1. 1. A multicatalytic proteinase (MCP) was purified from carp muscle by chromatography of DEAE-cellulose, hydroxylapatite and AcA34 to homogeneous. 2. 2. This MCP had three distinct catalytic activities, endopeptidase, trypsin-like and chymotrypsin-like activities and all activities were latent. 3. 3. Heating at 65°C induced all activities, whereas addition of sodium dodecyl sulfate induced only chymotrypsin-like activity. Therefore, it was postulated that the degree of latency is different among the catalytic activities. 4. 4. The endopeptidase activity of carp muscle MCP was different from mammalian MCPs. 5. 5. Judging from the equivocal effects of some reagents, the induced-MCP molecule itself is equipped with a regulating mechanism." @default.
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- W2034006508 date "1990-01-01" @default.
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- W2034006508 title "Induction of carp muscle multicatalytic proteinase activities by sodium dodecyl sulfate and heating" @default.
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- W2034006508 doi "https://doi.org/10.1016/0305-0491(90)90057-z" @default.
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