Abstract
The protein composition of Prunus armeniaca bark and leaf tissues was investigated by two-dimensional gel electrophoresis. Three different extraction procedures were tested in order to obtain reproducible gels with numerous spots of high intensity. The best results were achieved with extraction in Tris-buffer in the presence of a nonionic detergent, reducing agents, and polyphenol oxidase inhibitors. As many as 744 protein spots were resolved from leaf tissues. The patterns exhibited well-focused spots, with apparent molecular masses ranging from 19 to 90 kDa and isoelectric point from 4.5 to 8.5. The Tris extraction buffer was also the most appropriate for cortical tissue analysis.
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