Abstract
Two kinds of tubulin (α and β) have been described in microtubules from many different systems. In this study a discontinuous acrylamide-gel system containing sodium dodecyl sulfate was used to separate milligram quantities of α- and β-tubulin from microtubules of chick-embryo brain and from outer doublets of sea-urchin sperm. The isolated tubulins were characterized by peptide mapping and automated sequencing of the first 25 NH 2 -terminal amino acids. Our results show that α- and β-tubulin are related but distinctly different proteins and that each one has been highly conserved in the course of evolution.
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Publication Info
- Year
- 1973
- Type
- article
- Volume
- 70
- Issue
- 12
- Pages
- 3594-3598
- Citations
- 163
- Access
- Closed
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Identifiers
- DOI
- 10.1073/pnas.70.12.3594