Purification and Characterization of Thiol Proteinase as a Nitrate Reductase-Inactivating Factor from Leaves of Hordeum distichum L.
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概要
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A thiol proteinase was purified 6,400-fold from leaves of Hordeum distichum L. by a sequence of ammonium sulfate fractionation, gel filtration, ion exchange chromatography, hydrophobic chromatography and chromatofocusing. This enzyme also had nitrate reductase (NR)-inactivating activity, which was associated with proteolytic activity in almost constant proportions during the purification procedures. Its molecular weight was estimated as 74,000 by gel filtration, and it had an isoelectric point of 4.05 and an apparent K_m of 0.83 mg ml^<-1> for azocasein. The respective optimum pH for proteolytic and NR-inactivating activities were 6.0 and 7.0. On electrophoresis, the proteinase gave a major band that coincided with both activities; it also produced a faint band associated with no activity. Our purified thiol proteinase inactivated FMNH_2-NR and MVH-NR as well as NADH-NR, but it had only a slight effect on NADH cytochrome c reductase activity. This enzyme also inactivated glutamine synthetase.
- 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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