Action of Thiol Proteinase on Nitrate Reductase in Leaves of Hordeum distichum L.
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概要
- 論文の詳細を見る
Nitrate reductase (NR) from the leaves of Hordeum distichum was very susceptible to inactivation by barley leaf thiol proteinase, trypsin, and papain. A cytochrome c reductase species with a molecular weight of about 40,000 was derived from the NR complex by the proteolytic actions. The barley proteinase seemed to attack thc Mo^+-containing component of NR, just like trypsin and papain. It showed a preference for the alanine and tryptophan esters among the carbobenzoxyamino acid-nitrophenyl esters tested. In vivo NR activity in the presence of leupeptin was fairly higher than that in its absence. Leupeptin also protected NR from its cleavage to small cytochrome c reductase species, suggesting that the barley proteinase may play a role in the in vivo change in NR activity.
- 日本植物生理学会の論文
著者
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OJI Yoshikiyo
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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Oji Yoshikiyo
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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Hamano Takashi
Public Health Research Institute Of Kobe City
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Okamoto Saburo
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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Mitsuhashi Yukimasa
Public Health Research Institute of Kobe City
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Matsuki Yukio
Public Health Research Institute of Kobe City
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Okamoto Saburo
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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