Fluorescence approaches to the study of the p21ras GTPase mechanism

Biochem Soc Trans. 1991 Apr;19(2):432-7. doi: 10.1042/bst0190432.


The use of ribose-modified guanine nucleotides and tryptophan mutants of p21ras, neither of which have significant effect on the kinetic mechanism of the p21ras GTPase and the GAP-activated p21ras GTPase, will now allow a detailed kinetic study of how GAP and other regulatory proteins interact with p21ras. This will lead to a better understanding of how the relative concentrations of 'active' p21ras. GTP and 'inactive' p21ras. GDP are regulated in the cell.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • GTP Phosphohydrolases / metabolism*
  • GTPase-Activating Proteins
  • Kinetics
  • Mutagenesis, Site-Directed
  • Proteins / metabolism*
  • Proto-Oncogene Proteins p21(ras) / genetics
  • Proto-Oncogene Proteins p21(ras) / metabolism*
  • Spectrometry, Fluorescence / methods
  • ras GTPase-Activating Proteins


  • GTPase-Activating Proteins
  • Proteins
  • ras GTPase-Activating Proteins
  • GTP Phosphohydrolases
  • Proto-Oncogene Proteins p21(ras)