Purification of chitinolytic protein from Rehmannia glutinosa showing N-terminal amino acid sequence similarity to thaumatin-like proteins.
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.
Pan
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Department of Agricultural Chemistry, College of Agriculture and Life Sciences, Seoul National University, Suwon, Korea.
Lee
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Chae
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Kim
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D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D002686:Chitin / Q000737:chemistry*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D019657:Solanaceae / Q000737:chemistry*; D013549:Sweetening Agents
C121322:P1 protein, Rehmannia glutinosa; D010940:Plant Proteins; D013549:Sweetening Agents; D002686:Chitin; C003427:thaumatin protein, plant; D000645:Ammonium Sulfate