Purification of Chitinolytic Protein from Rehmannia glutinosa Showing N-terminal Amino Acid Sequence Similarity to Thaumatin-Like Proteins
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概要
- 論文の詳細を見る
We have purified a 21-kDa protein, designated as P1,from Rehmannia glutinosa to homogeneity by ammonium sulfate precipitation, anion exchange chromatography, hydrophobic interaction chromatography, and preparative native PAGE. The purified P1 had chitin degradation activity. The N-terminal amino acid sequence of P1 indicated that it is very similar to those of thaumatin and other reported thaumatin-like proteins.
- 社団法人日本農芸化学会の論文
- 1999-06-23
著者
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Pan C‐h
Seoul National Univ. Suwon Kor
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Kim S‐i
Seoul National Univ. Suwon Kor
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Pan Cheol-ho
Department Of Agricultural Chemistry And Research Center For New Bio-materials In Agriculture Colleg
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Lee Euna
Department Of Agricultural Chemistry And Research Center For New Bio-materials In Agriculture Colleg
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PAN CheolHo
Department of Agricultural Chemistry and Research Center for New Bio-Materials in Agriculture, Colle
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KIM SuIl
Department of Agricultural Chemistry and Research Center for New Bio-Materials in Agriculture, Colle
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CHAE YoungAm
Department of Agricultural Chemistry and Research Center for New Bio-Materials in Agriculture, Colle
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Chae Youngam
Department Of Agricultural Chemistry And Research Center For New Bio-materials In Agriculture Colleg
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Lee Eun-A
Department of Agricultural Chemistry and Research Center for New Bio-Materials in Agriculture, College of Agriculture and Life Sciences, Seoul National University
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Chae Young-Am
Department of Agricultural Chemistry and Research Center for New Bio-Materials in Agriculture, College of Agriculture and Life Sciences, Seoul National University
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- Purification of Chitinolytic Protein from Rehmannia glutinosa Showing N-terminal Amino Acid Sequence Similarity to Thaumatin-Like Proteins
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