Biochemical characterization of Artemia ras p21

Mol Cell Biochem. 1992 May 13;112(1):29-33. doi: 10.1007/BF00229640.

Abstract

The biochemical properties of Artemia ras proteins (p21) have been studied after immunoprecipitation with the monoclonal antibody Y13-259. The ras products bind GTP and GDP, and have GTPase activity. Artemia p21 was unable to hydrolyze Gp4G, although this dinucleotide exhibits high affinity for the protein. Our results demonstrate that the protein(s) recognized by the Y13-259 antibody in this crustacean behave as typical mammalian ras p21s.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Artemia / chemistry*
  • Binding, Competitive
  • Dinucleoside Phosphates / metabolism
  • GTP Phosphohydrolases / analysis
  • Guanosine Triphosphate / metabolism
  • Precipitin Tests
  • Proto-Oncogene Proteins p21(ras) / chemistry*
  • Proto-Oncogene Proteins p21(ras) / immunology
  • Substrate Specificity

Substances

  • Dinucleoside Phosphates
  • diguanosine tetraphosphate
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • Proto-Oncogene Proteins p21(ras)