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Gene expression in Acetabularia. I. Calibration of wheat germ cell-free translation system proteins as internal references for two-dimensional electrophoresis

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Shoeman,  Robert L.
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society;

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http://jcs.biologists.org/content/58/1/23.full.pdf
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Zitation

Shoeman, R. L., & Schweiger, H. (1982). Gene expression in Acetabularia. I. Calibration of wheat germ cell-free translation system proteins as internal references for two-dimensional electrophoresis. Journal of Cell Science, 58(1), 23-33. Retrieved from http://jcs.biologists.org/content/58/1/23.


Zitierlink: https://hdl.handle.net/21.11116/0000-0000-E8CA-7
Zusammenfassung
Modification of existing two-dimensional techniques enables isoelectric focusing and sodium dodecyl sulphate polyacrylamide gel electrophoresis of complex mixtures of proteins to be completed within 8 h. The method was optimized to separate the protein components of a wheat germ cell-free translation system, providing a statistically proven resolution better than 0 . 03 of a pH unit for the isoelectric point and 1000 for Mr. Fourteen of the more than 300 proteins separated were characterized with respect to Mr and isoelectric point relative to standard proteins under the same conditions. Stained wheat germ proteins thus serve as internal standards for analysis of in vitro translation products.