Skip to main content
SpringerLink
Log in

Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel

  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Summary

Separation of the proteins from rat liver 40S and 60S ribosomal subunits and polysomes was done in four different two-dimensional polyacrylamide gel electrophoresis systems. The first dimension was run at acidic or basic pH, the second dimension either with sodium dodecyl sulphate or at acidic pH in 18% acrylamide. The position of each individual protein of both subunits and polysomes was determined in each system. This identification resulted from a new method avoiding any previous purification of individual proteins. The new “proposed uniform nomenclature for mammalian ribosomal proteins” (McConkey et al. in press) was used for numbering the proteins in the four systems.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Arosio, P.A., Adelman, T.G., Drysdale, J.W.: On ferritin heterogeneity. Further evidence for heteropolymers. J. Biol. Chem. 253, 4451–4458 (1978)

    Google Scholar 

  • Arpin, M., Madjar, J.J., Reboud, J.P.: Occurence of phosphorylated forms of an acidic protein in the large ribosomal subunit of rat liver. Biochim. Biophys. Acta 519, 537–541 (1978)

    Google Scholar 

  • Banker, G.A., Cotman, C.W.: Measurement of free electrophoretic mobility and retardation coefficient of protein-sodium dodecyl sulfate complexes by gel electrophoresis. J. Biol. Chem. 247, 5856–5861 (1972)

    Google Scholar 

  • Blobel, G., Sabatini, D.D.: Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes. J. Cell Biol. 45, 130–145 (1970)

    Google Scholar 

  • Blobel, G., Sabatini, D.D.: Dissociation of mammalian polyribosomes into subunits by puromycin. Proc. Natl. Acad. Sci. U.S.A. 68, 390–394 (1971)

    Google Scholar 

  • Cenatiempo, Y., Cozzone, A.J., Genot, A., Reboud, J.P.: In vitro phosphorylation of proteins from free and membrane-bound rat liver polysomes. FEBS Lett. 79, 165–169 (1977)

    Google Scholar 

  • Collatz, E., Ulbrich, N., Tsurugi, K., Lightfoot, H.N., McKinlay, W., Lin, A., Wool, I.G.: Isolation of eukaryotic ribosomal proteins. J. Biol. Chem. 252, 9071–9080 (1977)

    Google Scholar 

  • Collatz, E., Wool, I.G., Lin, A., Stöffler, G.: The isolation of eukaryotic ribosomal proteins. J. Biol. Chem. 251, 4666–4672 (1976)

    Google Scholar 

  • Genot, A., Reboud, J.P., Cenatiempo, Y., Cozzone, A.J.: Endogenous phosphorylation of ribosomal proteins from membrane-free rat liver polysomes. FEBS Lett. 86, 103–107 (1978)

    Google Scholar 

  • Hanson, M.R., Davidson, J.N., Mets, L.J., Bogorad, L.: Characterization of chloroplast and cytoplasmic ribosomal proteins of Chlamydomonas reinhardi by two-dimensional gel electrophoresis. Mol. Gen. Genet. 132, 105–118 (1974)

    Google Scholar 

  • Harrison, P.M., Gregory, D.W.: Reassembly of apoferritin molecules from subunits. Nature 220, 578–580 (1968)

    Google Scholar 

  • Hoffman, W.L., Ilan, J.: Complete solubilization of ribosomal proteins during the fractionation of mouse liver ribosomal proteins by two-dimensional polyacrylamide gel electrophoresis. Prep. Biochem. 6, 13–26 (1976)

    Google Scholar 

  • Horak, I., Shiffmann, D.: Acidic phosphoproteins of HeLa and rat 60S ribosomal subunits. FEBS Lett. 82, 82–84 (1977)

    Google Scholar 

  • Hultin, T., Sjöquist, A.: Two-dimensional gel electrophoresis of animal ribosomal proteins based on charge inversion. Anal. Biochem. 46, 342–346 (1972)

    Google Scholar 

  • Issinger, O.G., Beier, H.: Characterisation of ribosomal proteins from HeLa and Krebs II mouse ascites tumor cells by different two-dimensional polyacrylamide gel electrophoresis techniques. Mol. Gen. Genet. 160, 297–309 (1978)

    Google Scholar 

  • Kaltschmidt, E., Wittmann, H.G.: Ribosomal proteins, VII. Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Anal. Biochem. 36, 401–412 (1970)

    Google Scholar 

  • Knopf, U.C., Sommer, A., Kenny, J., Traut, R.R.: A new two-dimensional gel electrophoresis system for the analysis of complex protein mixtures: Application to the ribosome of E. coli. Mol. Biol. Rep. 2, 34–40 (1975)

    Google Scholar 

  • Kumar, A., Subramanian, A.R.: Ribosome assembly in HeLa cells: Labeling pattern of ribosomal proteins by two-dimensional resolution. J. Mol. Biol. 94, 409–423 (1975)

    Google Scholar 

  • Kyriakopoulos, A., Subramanian, A.R.: Positions of individual ribosomal proteins after two-dimensional electrophoresis by a sensitive procedure. Biochim. Biophys. Acta 474, 308–311 (1977)

    Google Scholar 

  • Lastick, S.M., McConkey, E.H.: Exchange and stability of HeLa ribosomal proteins in vivo. J. Biol. Chem. 251, 2867–2875 (1976)

    Google Scholar 

  • Lewis, J.A., Sabatini, D.D.: Proteins of rat liver free and membrane-bound ribosomes. Modification of two large sub-unit proteins by a factor detached from ribosomes at high ionic strength. Biochim. Biophys. Acta 478, 331–349 (1977)

    Google Scholar 

  • Madjar, J.J., Arpin, M., Reboud, J.P.: Comparison of the protein content of free and membrane-bound rat liver polysomes and of the derived subunits. Mol. Biol. Rep. 3, 289–296 (1977a)

    Google Scholar 

  • Madjar, J.J., Arpin, M., Reboud, J.P.: A simple water-cooled apparatus for two-dimensional gel electrophoresis. Anal. Biochem. 83, 304–310 (1977b)

    Google Scholar 

  • Madjar, J.J., Michel, S., Cozzone, A.J., Reboud, J.P.: A method to identify individual proteins in four different two-dimensional gel electrophoresis systems: Application to E. coli ribosomal proteins. Anal. Biochem. (in press)

  • Martini, O.H.W., Gould, H.J.: Enumeration of rabbit reticulocyte ribosomal proteins. J. Mol. Biol. 62, 403–405 (1971)

    Google Scholar 

  • Martini, O.H.W., Gould, H.J.: Characterisation of eukaryotic ribosomal proteins. Mol. Gen. Genet. 142, 299–316 (1975a)

    Google Scholar 

  • Martini, O.H.W., Gould, H.J.: Molecular weight distribution of ribosomal proteins from several vertebrate species. Mol. Gen. Genet. 142, 317–331 (1975b)

    Google Scholar 

  • McConkey, E.H., Bielka, H., Gordon, J., Lastick, S.M., Lin, A., Ogata, K., Reboud, J.P., Traugh, J.A., Traut, R.R., Warner, J.R., Welfle, H., Wool, I.G.: Proposed uniform nomenclature for mammalian ribosomal proteins. Mol. Gen. Genet., in press (1979)

  • Mets, L.J., Bogorad, L.: Two-dimensional polyacrylamide gel electrophoresis: An improved method for ribosomal proteins. Anal. Biochem. 57, 200–210 (1974)

    Google Scholar 

  • Neville, D.M., Jr.: Molecular weight determination of protein dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. J. Biol. Chem. 246, 6328–6334 (1974)

    Google Scholar 

  • O'Farrell, P.H.: High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007–4021 (1975)

    Google Scholar 

  • Reyes, R., Vazquez, D., Ballesta, J.P.G.: Activities of nucleo-protein particles derived from rat liver ribosome. Biochim. Biophys. Acta 435, 317–332 (1976)

    Google Scholar 

  • Sherton, C.C., Wool, I.G.: Determination of the number of proteins in liver ribosomes and ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis. J. Biol. Chem. 247, 4460–4467 (1972)

    Google Scholar 

  • Sherton, C.C., Wool, I.G.: A comparison of the proteins of rat skeletal muscle and liver ribosomes by two-dimensional polyacrylamide gel electrophoresis. J. Biol. Chem. 249, 2258–2267 (1974a)

    Google Scholar 

  • Sherton, C.C., Wool, I.G.: Two-dimensional polyacrylamide gel electrophoresis of eukaryotic ribosomal proteins. Methods Enzymol. 30, 506–526 (1974b)

    Google Scholar 

  • Stöffler, G., Wool, I.G., Lin, A., Rak, K.H.: The identification of the eukaryotic ribosomal proteins homologous with Escherichia coli proteins L7 and L12. Proc. Natl. Acad. Sci. (U.S.A.) 71, 4723–4726 (1974)

    Google Scholar 

  • Subramanian, A.R.: Sensitive separation procedure for Escherichia coli ribosomal proteins and the resolution of high molecular weight components. Eur. J. Biochem. 45, 541–546 (1974)

    Google Scholar 

  • Subramanian, A.R., Gilbert, J.M., Kumar, A.: Comparison of ribosomal proteins from neoplastic and non-neoplastic cells. Resolution by two-dimensional gel electrophoresis. Biochim. Biophys. Acta 383, 93–96 (1975)

    Google Scholar 

  • Subramanian, A.R., Henshaw, E.C.: Variations in the protein pattern of Ehrlich ascites tumor cell polyribosomes. Biochim. Biophys. Acta 520, 203–209 (1978)

    Google Scholar 

  • Takanami, M.: A stable ribonucleoprotein for amino acid incorporation. Biochim. Biophys. Acta 39, 318–326 (1960)

    Google Scholar 

  • Terao, K., Ogata, K.: Studies on structural proteins of the rat liver ribosomes. I. Molecular weights of the proteins of large and small subunits. Biochim. Biophys. Acta 402, 214–229 (1975)

    Google Scholar 

  • Tsurugi, K., Collatz, E., Todokoro, K., Ulbrich, N., Lightfoot, H.N., Wool, I.G.: Isolation of eukaryotic ribosomal proteins. J. Biol. Chem. 253, 946–955 (1978)

    Google Scholar 

  • Tsurugi, K., Collatz, E., Todokoro, K., Wool, I.G.: Isolation of eukaryotic ribosomal proteins. J. Biol. Chem. 252, 3961–3969 (1977)

    Google Scholar 

  • Tsurugi, K., Collatz, E., Wool, I.G., Lin, A.: Isolation of eukaryotic ribosomal proteins. J. Biol. Chem. 251, 7940–7946 (1976)

    Google Scholar 

  • Waller, J.P., Harris, J.I.: Studies on the composition of the protein from Escherichia coli ribosomes. Proc. Natl. Acad. Sci. U.S.A. 47, 18–23 (1961)

    Google Scholar 

  • Weber, K., Osborn, M.: The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406–4412 (1962)

    Google Scholar 

  • Welfle, H., Goerl, M., Bielka, H.: Number and molecular weights of the basic proteins of rat liver ribosomes. Mol. Gen. Genet. 163, 101–112 (1978)

    Google Scholar 

  • Wittmann, H.G.: Purification and identification of Escherichia coli ribosomal proteins. In: Ribosomes (Nomura, M., Tissières, A., Lengyel, P., eds), pp. 93–114. New York: Cold Spring Harbor Laboratory 1974

    Google Scholar 

  • Wool, I.G., Stöffler, G.: Structure and function of eukaryotic ribosomes. In: Ribosomes (Nomura, M., Tissières, A., Lengyel, P., eds). pp. 417–460. New York: Cold Spring Harbor Laboratory 1974

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratoire de Biochimie Médicale, Université Lyon I, 43, Boulevard du 11 Novembre 1918, F-69621, Villeurbanne, (France)

    Jean-Jacques Madjar, Monique Arpin, Monique Buisson & Jean-Paul Reboud

Authors
  1. Jean-Jacques Madjar
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Monique Arpin
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Monique Buisson
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Jean-Paul Reboud
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Communicated by H.G. Wittmann

Rights and permissions

Reprints and permissions

About this article

Cite this article

Madjar, JJ., Arpin, M., Buisson, M. et al. Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel. Molec. Gen. Genet. 171, 121–134 (1979). https://doi.org/10.1007/BF00269998

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00269998

Keywords

Search

Navigation