Detection of novel guanine nucleotide binding proteins in bovine retinal rod outer segments

Biochem Biophys Res Commun. 1990 Jul 31;170(2):719-25. doi: 10.1016/0006-291x(90)92150-x.

Abstract

In the rod outer segment membranes of the bovine retina at least two members of the small molecular weight guanine nucleotide binding proteins were identified by means of the technique of binding radiolabeled GTP to nitrocellulose Western blots of proteins separated by sodium dodecyl sulphate gel electrophoresis. Such proteins, of 23 and 25 kDa, are able to specifically bind guanine nucleotides after denaturing treatments, and are not labeled by pertussis or cholera toxin-catalyzed ADP-ribosylation. The binding site is specific for GTP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism
  • Animals
  • Antibodies, Monoclonal / immunology
  • Binding Sites
  • Blotting, Western
  • Cattle
  • Cholera / metabolism
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • GTP-Binding Proteins / analysis*
  • Guanosine Triphosphate / metabolism
  • Molecular Weight
  • Pertussis Toxin
  • Photoreceptor Cells / analysis*
  • Rod Cell Outer Segment / analysis*
  • Transducin / immunology
  • Virulence Factors, Bordetella / metabolism

Substances

  • Antibodies, Monoclonal
  • Virulence Factors, Bordetella
  • Adenosine Diphosphate Ribose
  • Guanosine Triphosphate
  • Pertussis Toxin
  • GTP-Binding Proteins
  • Transducin