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Cited by 548

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THE MECHANISM OF ACTION OF COLCHICINE

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Borisy, G. G., Taylor, E. W.·1967·The Journal of Cell Biology

Abstract

Colchicine forms a complex in vivo with a protein present in fertilized or unfertilized sea urchin eggs; similar binding was obtained in vitro with the soluble fraction from egg homogenates. Kinetic parameters and binding equilibrium constant were essentially the same in vivo and in vitro. The binding site protein was shown to have a sedimentation constant of 6S by zone centrifugation. The protein was present in extracts of the isolated mitotic apparatus at a concentration which was several times higher than in whole-egg homogenates. It was extracted from the mitotic apparatus at low ionic strength under conditions which lead to the disappearance of microtubules. No binding could be detected to the 27S protein, previously described by Kane, which is a major protein component of the isolated mitotic apparatus. The properties of the colchicine-bindinG protein, (binding constant, sedimentation constant, Sephadex elution volume) are similar to those obtained with the protein from mammalian cells, sea-urchin sperm tails, and brain tissue, and thus support the conclusion that the protein is a subunit of microtubules.

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Metadata

Authors
Borisy, G. G., & Taylor, E. W.
Venue
The Journal of Cell Biology
Published
1967-08-01
Volume
34
Issue
2
Pages
535-548
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2132433230
Cited by
548
References
0
FWCI
21.98
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: THE MECHANISM OF ACTION OF COLCHICINE. https://app.cochat.ai/papers/10.1083/jcb.34.2.535
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Borisy, G. G., & Taylor, E. W. (1967). THE MECHANISM OF ACTION OF COLCHICINE. The Journal of Cell Biology. https://doi.org/10.1083/jcb.34.2.535

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.