Immunological comparison of purified DNA polymerase alpha from embryos of Drosophila melanogaster with forms of the enzyme present in vivo

J Biol Chem. 1982 Oct 25;257(20):12394-8.

Abstract

Specific antisera to purified DNA polymerase alpha from embryos of Drosophila melanogaster and to two of the four constituent subunits (alpha, beta, gamma, and delta) were prepared. These antibodies have revealed the following features of the enzyme. (i) The Mr = 148,000 alpha subunit is very likely derived by in vitro proteolysis from polypeptides with molecular weights of 185,000 and 166,000 that are present in vivo. (ii) The Mr = 60,000 beta subunit occurs in rapidly replicating embryos as both an 85,000- and a 60,000-dalton form, but predominantly as a 60,000-dalton form in more slowly replicating cultured cells. (iii) There is no detectable immunologic cross-reactivity between the four subunits. (iv) There is an abundance of antigenic material in embryos that co-migrates with the delta subunit of the purified enzyme during polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • DNA Polymerase II / isolation & purification*
  • DNA-Directed DNA Polymerase / isolation & purification*
  • Drosophila melanogaster / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Isoenzymes / analysis
  • Macromolecular Substances
  • Molecular Weight

Substances

  • Isoenzymes
  • Macromolecular Substances
  • DNA Polymerase II
  • DNA-Directed DNA Polymerase