Purification and Characterization of Intracellular Cysteine Protease Inhibitor from Chlorella sp
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概要
- 論文の詳細を見る
An intracellular cysteine protease inhibitor (ICPI) from Chlorella sp. was purified to homogeneity judging from polyacrylamide gel electrophoresis. The purified inhibitor had a molecular mass of 410kDa and a pI of 5.3. ICPI retained 100% of the original activity even after heating at 100℃ for 5 min. It exhibited an inhibitory activity against the proteolytic activity of papain, ficin, chymopapain, calcium dependent neutral protease and bromelain, but not against cathepsin B, pepsin, trypsin, or α-chymotrypsin. The inhibitory activity was inactivated by α-chymotrypsin. ICPI contained 76% carbohydrate residues by weight and inhibited papain at a ratio of 1:3. From these results, we assume that ICPI is a novel type of cysteine protease inhibitor.
- 社団法人 日本食品科学工学会の論文
- 1999-05-01
著者
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Atta Kazusi
Department Of Bioscience And Biotechnology Faculty Of Agriculture University Of The Ryukyus
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Ishihara M
Laboratory Of Protein Chemistry And Engineering Graduate School Of Bioresource And Environmental Sci
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Ishihara Masanobu
Department Of Bioscience And Biotechnology Faculty Of Agriculture Ryukyu University
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Toyama Seizen
Department Of Bioscience And Biotechnology Faculty Of Agriculture University Of The Ryukyus
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Tawata S
Univ. Ryukyus Okinawa Jpn
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Tawata Shinkichi
Department Of Bioscience And Biotechnology College Of Agriculture University Of Ryukyus
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TOYAMA Seizen
Department of Agricultural Chemistry, University of the Ryukyus
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