Action of Thiol Proteinase on Nitrate Reductase in Leaves of Hordeum distichum L. |
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| Authors: | Hamano, Takashi Oji, Yoshikiyo Mitsuhashi, Yukimasa Matsuki, Yukio Okamoto, Saburo |
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| Affiliation: | 1Public Health Research Institute of Kobe City Minatozimanaka-cho 4-6, Chuo-ku, Kobe 650, Japan
2Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University Rokkodai-cho 1-1, Nada-ku, Kobe 657, Japan |
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| Abstract: | Nitrate reductase (NR) from the leaves of Hordeum distichumwas very susceptible to inactivation by barley leaf thiol proteinase,trypsin, and papain. A cytochrome c reductase species with amolecular weight of about 40,000 was derived from the NR complexby the proteolytic actions. The barley proteinase seemed toattack the Mo+-containing component of NR, just like trypsinand papain. It showed a preference for the alanine and tryptophanesters among the carbobenzoxyamino acid-nitrophenylesters tested. In vivo NR activity in the presence of leupeptin was fairlyhigher than that in its absence. Leupeptin also protected NRfrom its cleavage to small cytochrome c reductase species, suggestingthat the barley proteinase may play a role in the in vivo changein NR activity. (Received May 21, 1984; Accepted September 10, 1984) |
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