Structural and functional analysis of yeast ribosomal proteins.
作者： H.A. Raué , W.H. Mager , R.J. Planta
DOI: 10.1016/0076-6879(91)94035-B
关键词:
摘要: Publisher Summary This chapter describes the structural and functional analysis of yeast ribosomal proteins. Ribosomal proteins have been separated characterized predominantly by various types two-dimensional gel electrophoresis, all which are modifications procedures developed Kaltschmidt Wittmann (basic urea/acidic urea) Mets Bogorad (acidic urea/sodium dodecyl sulfate) respectively, for Escherichia coli Best results obtained using procedure small subunit large Both separations can be carried out conveniently rapidly employing a minigel system. Functional in prokaryotes is based on ability to take prokaryotic subunits apart reassemble purified components into biologically active particles. Reconstitution eukaryotic confined reassociation only few proteins, dissociated from treatment (the split proteins), with resulting ribonucleoprotein core particle.
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