High-performance liquid chromatographic purification of a ribonucleoprotein complex and its protein component.
This paper describes the rapid purification by high-performance liquid chromatographic techniques of milligram quantities of the 7 S ribonucleoprotein complex ( RNP 7 S) and its protein component from tench (Tinca tinca) oocyte extracts. High-performance gel permeation chromatography (with a TSK 3000SW column) was found to be unacceptable because of multiple contaminants which coelute with RNP 7 S. In contrast, semipreparative high-performance DEAE ion-exchange chromatography was found to give an excellent separation of the 7 S complex which could be directly adapted to a preparative scale providing rapid purification (less than 1 h) of milligram quantities of the complex. Agarose electrophoresis followed by specific staining of protein and nucleic acid was found to be a convenient and rapid means of evaluating the purification. Finally, reverse-phase high-performance liquid chromatography was found suitable for the purification of the protein component of the 7 S complex.[1]References
- High-performance liquid chromatographic purification of a ribonucleoprotein complex and its protein component. Monteilhet, C., Aggerbeck, L.P. Anal. Biochem. (1986) [Pubmed]
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