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  • Title: Characterization of a Gly19-->Val mutant of ram p25, a low Mr GTP-binding protein: loss of GTP/GDP-binding activity in the mutated ram p25.
    Author: Nagata K, Suzuki T, Okano Y, Hamaguchi M, Nozawa Y.
    Journal: Biochem Biophys Res Commun; 1992 Nov 30; 189(1):330-5. PubMed ID: 1449488.
    Abstract:
    A substitution of Gly for Val at position 19, which corresponds to oncogenic Gly13-->Val mutation of ras p21, was introduced in a low Mr GTP-binding protein, ram p25. The protein was expressed in cytosolic fraction of Escherichia coli and purified by using specific antibody raised against ram p25. The mutated protein had no guanine nucleotide-binding activity although [Val13]ras p21 was reported to have. The analysis of guanine nucleotide composition of the purified [Val19]ram p25 revealed that the protein was free of nucleotide whereas the normal ram p25 bound about 1 mol of GDP per mol of protein. These results strongly suggested that some part(s) of variable regions as well as the consensus regions are important for the biochemical properties of ram p25.
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