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Nucleoside diphosphate (NDP) kinase has been postulated to generate GTP from the GDP bound to tubulin. The purified chick brain enzyme was studied with respect to its kinetic parameters, and the protein-protein interactions between the NDP kinase and tubulin were examined. No specific interaction is observed between the enzyme and assembled microtubules, tubulin dimers, or tubulin-microtubule-associated protein (MAP) oligomers under a variety of nucleotide conditions. The apparent association is demonstrated to result from NDP kinase binding to a co-purifying contaminant. The absence of detectable NDP kinase-tubulin interactions indicates that NDP kinase does not directly charge up tubulin-GDP.
K Islam, and
R G Burns
September 1984,
The Journal of biological chemistry,
K Islam, and
R G Burns
June 2011,
Molecular and biochemical parasitology,
K Islam, and
R G Burns
August 1992,
Biochemical and biophysical research communications,
K Islam, and
R G Burns
January 2004,
Methods in enzymology,
K Islam, and
R G Burns
October 1984,
European journal of biochemistry,
K Islam, and
R G Burns
October 1979,
The Journal of biological chemistry,
K Islam, and
R G Burns
May 1988,
FEBS letters,
K Islam, and
R G Burns
February 1995,
Current opinion in cell biology,
K Islam, and
R G Burns
June 2018,
Cold Spring Harbor perspectives in biology,
K Islam, and
R G Burns
January 2008,
Biofizika,
