一种玉米脱水蛋白的纯化
Purification of a maize dehydrin.
作者信息
Ceccardi T L, Meyer N C, Close T J
机构信息
Department of Botany and Plant Sciences, University of California, Riverside 92521-0124.
出版信息
Protein Expr Purif. 1994 Jun;5(3):266-9. doi: 10.1006/prep.1994.1040.
A maize dehydrin with an apparent molecular weight of 20 kDa was purified from whole kernels of maize inbred line G50. Kernels were ground in a seed mill, stirred overnight in extraction buffer, and centrifuged to extract soluble proteins. The sample was heated to 89 degrees C and centrifuged to remove heat-insoluble proteins. The remaining soluble proteins were fractionated in a three-step chromatographic process. Following cation exchange, hydrophobic interaction, and gel filtration chromatography, pure dehydrin samples were obtained.
从玉米自交系G50的全籽粒中纯化出一种表观分子量为20 kDa的玉米脱水蛋白。籽粒在种子研磨机中研磨，在提取缓冲液中搅拌过夜，然后离心以提取可溶性蛋白质。将样品加热至89摄氏度并离心以去除热不溶性蛋白质。剩余的可溶性蛋白质通过三步色谱法进行分离。经过阳离子交换、疏水相互作用和凝胶过滤色谱后，获得了纯的脱水蛋白样品。
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