Charge effect on the colchicine binding-site of tubulin
Roychowdhuri, S.; Banerjee, A.; Bhattacharyya, B.
Biochemical and Biophysical Research Communications 113(2): 384-390
1983
ISSN/ISBN: 0006-291X PMID: 6870862 Document Number: 201847
Poly(L-lysine) enhanced colchicine binding to brain tubulin several fold. Bases of biological interest that were tested and found to be inactive were spermine, spermidine and L-lysine. Part of this enhanced binding is due to the increase in the affinity of colchicine-tubulin interaction in the presence of poly(L-lysine). Moreover, poly(L-lysine) stabilized the colchicine binding site of tubulin against thermal denaturation.