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Radioiodination of proteins in single polyacrylamide-gel slices - tryptic peptide analysis of all major members of complex multicomponent systems using microgram quantities of total protein

Academic Article
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Overview

authors

  • Elder, John
  • Pickett, R. A.
  • Hampton, J.
  • Lerner, Richard

publication date

  • 1977

journal

  • Journal of Biological Chemistry  Journal

abstract

  • A method is described for radioiodination to high specific activity of fixed and stained proteins within sodium dodecyl sulfate-polyacrylamide gels, without elution of the proteins from the gel. Following radioiodination, the proteins can be removed from the gel by trypsin treatment and the peptides analyzed. This procedure offers a means to structurally compare the proteins of multicomponent systems when purification of each component to homogeneity is unfeasible. Using this technique, we have compared the tryptic peptides of all the major protein components of Moloney and Rauscher leukemia viruses using only 50 to 100 microgram of total protein from each virus. Additionally, we have analyzed the membrane proteins of Dictyostelium discoideum at various stages in development. The validity of the technique and its value as a tool for comparative studies and identification of precursor-product relationships is discussed.

subject areas

  • Dictyostelium
  • Electrophoresis, Polyacrylamide Gel
  • Fungal Proteins
  • Iodine Radioisotopes
  • Isotope Labeling
  • Membrane Proteins
  • Microchemistry
  • Moloney murine leukemia virus
  • Peptide Fragments
  • Proteins
  • Rauscher Virus
  • Sodium Dodecyl Sulfate
  • Trypsin
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 893422
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Additional Document Info

start page

  • 6510

end page

  • 6515

volume

  • 252

issue

  • 18

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