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Research Article| Volume 258, ISSUE 1, P24-26, January 10, 1983

Antibodies to calf thymus RNA polymerase II from egg yolks of immunized hens.

Open AccessPublished:January 10, 1983DOI:https://doi.org/10.1016/S0021-9258(18)33211-3
Antibodies to calf thymus RNA polymerase II from egg yolks of immunized hens.
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      Polyclonal antibodies to calf thymus RNA polymerase II were raised in laying hens. Up to 75 mg of immunoglobulin/egg yolk were extracted by the polyethylene glycol procedure of Roeder (Roeder, R.G. (1976) in RNA Polymerase (Losick, R., and Chamberlin, M., eds) pp. 285-330, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY). The concentration of specific antibody in egg yolks (IgY) was comparable to that of serum as measured by enzyme-linked immunoassay. Purified antibody was shown to be directed against enzyme by removal of enzyme activity in immune complexes precipitated by rabbit anti-chicken IgY. The antibodies recognized several of the subunits of the enzyme as determined by their reactivity with polypeptides transferred to nitrocellulose paper after gradient sodium dodecyl sulfate-gel electrophoresis. Production of antibodies in laying hens may facilitate the study of other highly conserved antigens that are poorly immunogenic in mammalian hosts.

      REFERENCES

        • Poison A.
        • von Wechmar M.B.
        • van Regenmortel M.H.V.
        Immunol. Commun. 1980; 9: 475-493
        • Roeder R.G.
        Losick R. Chamberlin M. RNA Polymerase. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY1976: 285-330
        • Zillig W.
        • Palm P.
        • Heil A.
        Losick R. Chamberlin M. RNA Polymerase. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY1976: 101-125
        • Ruet A.
        • Sentenac A.
        • Fromageot P.
        • Winsor B.
        • Lacroute F.
        J. Biol. Chem. 1980; 255: 6450-6455
        • Greenleaf A.
        • Weeks J.
        • Voelker R.
        • Ohnishi S.
        • Dickson B.
        Cell. 1980; 21: 785-792
        • Brodner O.
        • Wieland T.
        Biochemistry. 1976; 15: 3480-3484
        • Jamrick M.
        • Greenleaf A.L.
        • Bautz E.K.F.
        Proc. Natl. Acad. Sci. U. S. A. 1977; 74: 2079-2083
        • Buhler J.-M.
        • Huet J.
        • Davies K.
        • Sentenac A.
        • Fromageot P.
        J. Biol. Chem. 1980; 255: 9949-9954
        • Weeks J.
        • Coulter D.
        • Greenleaf A.
        J. Biol. Chem. 1982; 257: 5884-5891
        • Kramer A.
        • Bautz E.K.F.
        Eur. J. Biochem. 1981; 117: 449-455
        • Ingles C.J.
        Biochem. Biophys. Res. Commun. 1973; 55: 364-371
        • Huet J.
        • Sentenac A.
        • Fromageot P.
        J. Biol. Chem. 1982; 257: 2613-2618
        • Kramer A.
        • Haars R.
        • Kabisch R.
        • Will H.
        • Bautz F.
        • Bautz E.K.F.
        Mol. Gen. Genet. 1980; 180: 193-199
        • Christmann J.L.
        • Dahmus M.E.
        J. Biol. Chem. 1981; 256: 11798-11803
        • Carroll S.B.
        • Stollar B.D.
        Proc. Natl. Acad. Sci. U. S. A. 1982; (in press)
        • Hodo H.
        • Blatti S.P.
        Biochemistry. 1977; 16: 2334-2343
        • Weil P.A.
        • Blatti S.P.
        Biochemistry. 1975; 14: 1636-1642
        • Weber K.
        • Osborn M.
        Neurath H. Hill R.L. The Proteins. 3rd. Ed. Academic Press, New York1975: 179-223
        • Towbin H.
        • Staehelin T.
        • Gordon J.
        Proc. Natl. Acad. Sci. U. S. A. 1979; 76: 4350-4354
        • Hunter R.
        Proc. Soc. Exp. Biol. Med. 1970; 133: 989-992
        • Morrissey J.H.
        Anal. Biochem. 1981; 117: 307-310

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      Published online: January 10, 1983

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      DOI: https://doi.org/10.1016/S0021-9258(18)33211-3

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      © 1983 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

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