Abstract
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
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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GTP Phosphohydrolases / metabolism*
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GTPase-Activating Proteins
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Kinetics
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Mutagenesis, Site-Directed
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Proteins / metabolism*
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Proto-Oncogene Proteins p21(ras) / genetics
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Proto-Oncogene Proteins p21(ras) / metabolism*
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Spectrometry, Fluorescence / methods
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ras GTPase-Activating Proteins
Substances
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GTPase-Activating Proteins
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Proteins
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ras GTPase-Activating Proteins
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GTP Phosphohydrolases
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Proto-Oncogene Proteins p21(ras)