The extraction of proteins from eukaryotic ribosomes and ribosomal subunits View Full Text


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Article Info

DATE

1974-06

AUTHORS

Corinne C. Sherton, Ira G. Wool

ABSTRACT

Proteins were extracted from rat liver ribosomes and ribosomal subunits: with 67% acetic acid (in the presence of 3.3 mM, 33 mM, or 67 mM Mg) with 2 M LiCL in 4 M urea; with 0.25 N HCI; with 1% SDS; and after RNase digestion. The most efficient extraction and the best recovery were either with acetic acid in the presence of 33 mM or 67 mM Mg, or with LiCI-urea. Protein extracted with acetic acid, LiCi-urea, or with HCI had little or no contamination with RNA. The ribosomal proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis: the proteins extracted with acetic acid were the most soluble in the sample gel solution; their electrophoretograms displayed the maximum number of spots and the smallest number of derivatives or altered proteins. Preparations of protein extracted with SDS or RNase were relatively insoluble in the sample gel solution, and proteins extracted with HCI showed a large number of derivatives. All things considered, the most satisfactory method for the extraction of protein from eukaryotic ribosomes is with 67% acetic acid in the presence of 33 mM MgCl2. More... »

PAGES

97-112

References to SciGraph publications

  • 1973-12. Studies on proteins of animal ribosomes in MOLECULAR GENETICS AND GENOMICS
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00264778

    DOI

    http://dx.doi.org/10.1007/bf00264778

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/4457758


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