Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm,Nomuraea atypicola |
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| Authors: | Mitsuhiro Ueda Naomi Yamamoto Mizuho Kusuda Masami Nakazawa Shigeo Takenaka Kazutaka Miyatake Kenji Ouchi Minoru Sakaguchi Kuniyo Inouye |
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| Affiliation: | 1. Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan;2. Hokuto Corporation, Mushroom Research Laboratory, 800-8, Shimokomazawa, Naganoshi, Nagano, 381-0008, Japan;3. Laboratory of Cell Biology, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan;4. Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan |
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| Abstract: | A new protease was purified from the culture filtrate of a plant worm, Nomuraea atypicola. The activity of the protease was suppressed by metalloprotease inhibitors such as EDTA and 1,10-phenanthroline, suggesting that it might be a metalloprotease. Its molecular mass was estimated to be 48 kDa by SDS-PAGE, and its optimal pH and temperature were pH 8.5–9.0 and 40 °C, respectively. The N-terminal amino acid sequence of the metalloprotease was similar to those of fungalysin metallopeptidases of the M36 family from fungi such as Coccidioides posadasii, Pyrenophora tritici-repentis, and Arthroderma gypseum, supporting the idea that it is a fungalysin-like metallopeptidase. |
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