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 NH2-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.
Keywords: Strongylocentrotus, gel electrophoresis, protein sequencing, evolution
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