Isolation and characterization of a cysteine protease of freesia corms |
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Authors: | Uchikoba Tetsuya Okubo Michiko Arima Kazunari Yonezawa Hiroo |
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Institution: | Kagoshima University Musium, Japan. uchik@sci.kagoshima-u.ac.jp |
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Abstract: | A protease, freesia protease (FP)-A, was purified to electrophoretic homogeneity from regular freesia (Freesia reflacta) corms in harvest time. The Mr of FP-A was estimated to be 24 k by SDS-PAGE. The optimum pH of the enzyme was 8.0 using a casein substrate. These enzymes were strongly inhibited by p-chloromercuribenzoic acid but not by phenylmethane-sulfonylfluoride and EDTA. These results indicate that FP-A belongs to the cysteine proteases. The amino terminal sequence of FP-A was similar to that of papain, and the sequences was regarded to the conservative residues of cysteine protease. From the hydrolysis of peptidyl-p-NAs, the specificity of FP-A was found to be broad. It was thought that FP-A was a new protease from freesia corms. |
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