Purification of a maize dehydrin.
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.
Ceccardi
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Department of Botany and Plant Sciences, University of California, Riverside 92521-0124.
Meyer
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D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008970:Molecular Weight; D010940:Plant Proteins / Q000302:isolation & purification*; D012639:Seeds / Q000737:chemistry; D003313:Zea mays / Q000737:chemistry*
D010940:Plant Proteins