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- W1998300230 abstract "The cysteine proteinase of sprouting potato tubers was purified to homogeniety as judged by PAGE or SDS-PAGE for the first time. The molecular weight of this enzyme was 28,200 daltons by Sephadex G-75, and 27,500 daltons by SDS-PAGE. This enzyme has an isoelectric point at pH 5.10, an optimum pH for the activity at pH 5.0~6.0, and a tendency to stability between pH 4.5~6.5. SH-compounds such as DTT (dithiothreitol) and 2-mercaptoethanol 4.5 stimulated the activity of this enzyme. Heavy metal ions and Zn2+ strongly inhibited it, but EDTA slightly increased it. SH blocking reagents such as monoiodoacetate, PCMB, and TLCK inhibited this enzyme activity. Chymostatin, antipain, leupeptin and E64 caused complete inhibition." @default.
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- W1998300230 date "1986-01-01" @default.
- W1998300230 modified "2023-10-02" @default.
- W1998300230 title "Purification and properties of cysteine proteinase in sprouting potato tubers." @default.
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- W1998300230 doi "https://doi.org/10.1271/bbb1961.50.381" @default.
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