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Science 1 August 1969:
Vol. 165. no. 3892, pp. 498 - 499
DOI: 10.1126/science.165.3892.498
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Articles

Vinblastine-Induced Precipitation of Microtubule Protein

Robert Marantz 1, Martha Ventilla 2, and Michael Shelanski 3

1 Departments of Pathology and Pharmacology, Albert Einstein College of Medicine, Bronx., New York 10461
2 Department of Chemistry, Columbia University, New York, and Department of Pathology (Neuropathology), Albert Einstein College of Medicine
3 Department of Pathology (Neuropathology), Albert Einstein College of Medicine

Vinblastine quantitatively precipitates a protein from supernatants obtained from high-speed centrifugation of homogenates of HeLa cells and of pig brain. This protein migrates as a single band on gel electrophoresis, has a mobility identical to that of purified microtubule protein, and-like microtubule protein-binds colchicine. The precipitation is partially inhibited by 0.9 percent NaCl.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Microtubule Function in Immune and Nonimmune Lymphocyte-Mediated Cytotoxicity.
T. B. Strom, M. R. Garovoy, C. B. Carpenter, and J. P. Merrill (1973)
Science 181, 171-173
   Abstract »    PDF »
Effect of Colchicine, Colcemid, and Vinblastine on the Agglutination, by Concanavalin A, of Transformed Cells.
H. H. Yin, T. E. Ukena, and R. D. Berlin (1972)
Science 178, 867-868
   Abstract »    PDF »
Microtubular Protein: Synthesis and Metabolism in Developing Brain.
G. R. Dutton and S. Barondes (1969)
Science 166, 1637-1638
   Abstract »    PDF »
Induction in vitro of Microtubular Crystals by Vinca Alkaloids.
K. G. Bensch, R. Marantz, H. Wisniewski, and M. Shelanski (1969)
Science 165, 495-496
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)