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Vincristine-Induced Self-Association of Calf Brain Tubulin.

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Title Vincristine-Induced Self-Association of Calf Brain Tubulin.
 
Creator Prakash, V.
Timasheff, S. N.
 
Subject 01 Alkaloid Biochemistry
 
Description The vincristine-induced self-association of tubulin has been examined in a sedimentation velocity
study as a function of free drug concentration in PG buffer (0.01 M Napi and lo4 M GTP, pH 7.0) at
20 OC. Analysis of the weight-average sedimentation coefficient (Sz0,+,,) as a function of protein concentration
showed a good fit with the model of an indefinite, isodesmic self-association mechanism. Analysis of the
apparent association constants in terms of the Wyman linkage relations showed a good fit to mediation of
the self-association by the binding of one ligand molecule. The intrinsic association constant for dimerization
of the vincristine-liganded tubulin was found to be 3.8 X IO5 M-’, and the intrinsic equilibrium constant
for the binding of the self-association-linked vincristine molecule had a value of 3.5 X lo4 M-’, consistent
with that measured by fluorescence in our laboratory [Prakash, V., & Timasheff, S. N. (1983) J. Biol. Chem.
258, 1689-16971, Both reactions are stronger in the presence of vincristine than of vinblastine, reflecting
the oxidation of a -CH3 group to -CHO when going from the latter drug to the former one.
 
Date 1985
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/13546/1/Biochemistry%201985.pdf
Prakash, V. and Timasheff, S. N. (1985) Vincristine-Induced Self-Association of Calf Brain Tubulin. Biochemistry, 24. pp. 5004-5010. ISSN 0006-2960