Purification of Chitinolytic Protein from Rehmannia glutinosa Showing N-terminal Amino Acid Sequence Similarity to Thaumatin-Like Proteins

抄録

  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.