Isolation and Characterization of Basic Exochitinase from Leaf Extract of Rehmannia glutinosa
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概要
- 論文の詳細を見る
Rehmannia chitinases were extracted from the leaves of Rehmannia glutinosa under acidic conditions (pH 2.9). We purified a 28.6-kDa chitinase, designated as P2,from crude extract to homogeneity by (NH_4)_2SO_4 precipitation, chromatography with regenerated chitin affinity and hydrophobic interaction column, and preparative native PAGE. Isolated P2 showed maximum chitinase activity at pH 5.0 and 60℃, and had a isoelectric point of 8.46. P2 produced only (GlcNAc)_2 from (GlcNAc)_4-6 and regenerated chitin. Based on these results, we arrived at the conclusion that P2 was a basic exochitinase.
- 社団法人日本農芸化学会の論文
- 1999-10-23
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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SON JongMun
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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Son Jongmun
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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Son Jong-Mun
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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- Isolation and Characterization of Basic Exochitinase from Leaf Extract of Rehmannia glutinosa
- Purification of Chitinolytic Protein from Rehmannia glutinosa Showing N-terminal Amino Acid Sequence Similarity to Thaumatin-Like Proteins
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