Irreversible Potent Activation and Reversible Inhibition of Trypsin-Like Activity of 20S Proteasome Purified from Xenopus Oocytes by Fatty Acid
スポンサーリンク
概要
- 論文の詳細を見る
The 20S proteasome purified from animal cells has various latent peptidase activities. Fatty acids such as linoleic, linolenic and oleic acids strongly activate both the chymotrypsin-type and peptidylglutamylpeptide(PGP)hydrolase-type activities, but have been reported to have little activation or inhibition of the trypsin-type activity. We show here that an increase of the fatty acid concentration produces activation of chymotrypsin-type and PGP hydrolase-type in a biphasic fashion : no effect until the threshold concentration and then a sharp activation. In contrast, the trypsin-type activity was markedly inhibited at low concentrations of fatty acid, slightly activated at higher concentrations, and inhibited again at even higher concentrations. The inhibition was removed when the concentration of fatty acid was reduced by dilution after pre-incubation with the fatty acid. As a result, the activation pattern became biphasic, which was identical to that of chymotrypsin-type and PGP hydrolase-type activities. These results suggest that in the chymotrypsin-type and PGP hydrolase-type peptidases fatty acids bind first to a class of sites without direct effect on the peptidase activity, but after saturation of this class it permits more fatty acid to bind to another class of sites involved in the activation. In the trypsin-type peptidase an additional class of fatty acid binding sites is uniquely present, which is involved in the enzyme inhibition. The dilution procedure described above removes the fatty acid molecules bound to the inhibition sites, but not the fatty acid molecules bound to the activation sites ; this results in the fatty acid activation profile indistinguishable from that of the chymotrypsin and PGP hydrolase-type peptidases.
- 社団法人日本動物学会の論文
著者
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Yamada Junko
Department of Neurophysiology, Hirosaki University Graduate School of Medicine
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Sato Kenji
Department Of Food Sciences And Nutritional Health Kyoto Prefectural University
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Sato Katsuaki
Central Research Laboratories Of Ajinomoto Co. Inc.
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Yamada Junko
Department Of Biology And Geosciences Faculty Of Science Shizuoka University
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Kubota Satoshi
Division Of Human Health And Medical Science Graduate School Of Kuroshio Science Kochi University
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TOKUMOTO Toshinobu
Department of Biology, Faculty of Science, Shizuoka University
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YAMADA Shigehiro
ORYNOVA K. K.
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Sato K
Department Of Food Sciences And Nutritional Health Kyoto Prefectural University
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Kubota S
Division Of Human Health And Medical Science Graduate School Of Kuroshio Science Kochi University
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Yamada S
Department Of Biological Chemistry College Of Bioresource Sciences Nihon University:(present Address
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Sato Kentaro
Department Of Otorhinolaryngology Kanagawa Dental College
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Yamada Shinpei
Department Of Biorogy Faculty Of Science Shizuoka University
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Yamada Shinpei
Department Of Biology And Geoscience Faculty Of Science Shizuoka University
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Ishikawa K
Department Of Biology And Geosciences Faculty Of Science National University Corporation Shizuoka Un
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Yasutomi Masumi
Laboratory of Biology, Aichi Medical University
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Ishikawa Katsutosi
Department of Biology and Geosciences, Faculty of Science, Shizuoka University
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Yasutomi Masumi
Lab, of Biology, Aichigakuin university
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Yasutomi Masumi
Lab Of Biology Aichigakuin University
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Yasutomi Masumi
Laboratory Of Biology Aichi Medical University
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Yamada Junko
Department Of Biotechnology Graduate School Of Engineering Nagoya University
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Yamada S
Department Of Biology And Geosciences Faculty Of Science Shizuoka University
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Tokumoto Toshinobu
Department Of Biology And Geosciences Faculty Of Science National University Corporation Shizuoka Un
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