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COLCEMID INHIBITION OF CELL GROWTH AND THE CHARACTERIZATION OF A COLCEMID-BINDING ACTIVITY IN SACCHAROMYCES CEREVISIAE

COLCEMID INHIBITION OF CELL GROWTH AND THE CHARACTERIZATION OF A COLCEMID-BINDING ACTIVITY IN... Under restricted culture conditions, the growth and division of Saccharomyces cerevisiae was inhibited by the antimitotic drug Colcemid; in contrast, the related drug colchicine had no effect. The difference in the sensitivity of yeast to these two agents was not dependent on their ability to permeate the cell but rather reflected an inherent difference in the affinity of the two drugs for a cellular-binding site. The binding moiety was characterized by gel filtration as a macromolecule of approximately 110,000 mol wt with an affinity constant for Colcemid of 0.5 x 10 4 liters per mole; in addition, this macromolecule was retained by diethylaminoethyl (DEAE) ion exchangers. On the basis of these properties, the Colcemid-binding substance in S. cerevisiae cells was provisionally identified as microtubule subunits. Footnotes Submitted: 28 April 1972 Revision received 25 May 1972 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

COLCEMID INHIBITION OF CELL GROWTH AND THE CHARACTERIZATION OF A COLCEMID-BINDING ACTIVITY IN SACCHAROMYCES CEREVISIAE

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References (26)

Publisher
Rockefeller University Press
Copyright
© 1972 Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.55.2.355
Publisher site
See Article on Publisher Site

Abstract

Under restricted culture conditions, the growth and division of Saccharomyces cerevisiae was inhibited by the antimitotic drug Colcemid; in contrast, the related drug colchicine had no effect. The difference in the sensitivity of yeast to these two agents was not dependent on their ability to permeate the cell but rather reflected an inherent difference in the affinity of the two drugs for a cellular-binding site. The binding moiety was characterized by gel filtration as a macromolecule of approximately 110,000 mol wt with an affinity constant for Colcemid of 0.5 x 10 4 liters per mole; in addition, this macromolecule was retained by diethylaminoethyl (DEAE) ion exchangers. On the basis of these properties, the Colcemid-binding substance in S. cerevisiae cells was provisionally identified as microtubule subunits. Footnotes Submitted: 28 April 1972 Revision received 25 May 1972

Journal

The Journal of Cell Biology – Rockefeller University Press

Published: Nov 1, 1972

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