从地黄中纯化出与类甜蛋白具有N端氨基酸序列相似性的几丁质分解蛋白。
Purification of chitinolytic protein from Rehmannia glutinosa showing N-terminal amino acid sequence similarity to thaumatin-like proteins.
作者信息
Pan C H, Lee E A, Chae Y A, Kim S I
机构信息
Department of Agricultural Chemistry, College of Agriculture and Life Sciences, Seoul National University, Suwon, Korea.
出版信息
Biosci Biotechnol Biochem. 1999 Jun;63(6):1138-40. doi: 10.1271/bbb.63.1138.
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.
我们通过硫酸铵沉淀、阴离子交换色谱、疏水相互作用色谱和制备型天然聚丙烯酰胺凝胶电泳，从地黄中纯化出一种21 kDa的蛋白质，命名为P1，并使其达到了均一性。纯化后的P1具有几丁质降解活性。P1的N端氨基酸序列表明，它与奇异果甜蛋白及其他已报道的类奇异果甜蛋白非常相似。
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