Assembly of proteolytically cleaved tubulin.


Journal Article

Conditions have been found for limited proteolysis of purified tubulin, in which 70-90% of the molecules are cleaved at one or two sites. Thermolysin and chymotrypsin cleave the alpha and beta subunits, respectively, at single sites. Trypsin cleaves the alpha subunit at two sites. The chymotrypsin site and one of the trypsin sites are apparently inaccessible on assembled microtubules. The different samples of proteolyzed tubulin were all fully competent to assemble in a buffer containing 1 M sodium glutamate. In another buffer (50 mM morpholinoethanesulfonic acid, 3.4 M glycerol) tubulin digested by thermolysin assembled as well as native tubulin, but samples digested by chymotrypsin or trypsin would not assemble even at high protein concentrations.

Full Text

Duke Authors

Cited Authors

  • Brown, HR; Erickson, HP

Published Date

  • January 1, 1983

Published In

Volume / Issue

  • 220 / 1

Start / End Page

  • 46 - 51

PubMed ID

  • 6338834

Pubmed Central ID

  • 6338834

International Standard Serial Number (ISSN)

  • 0003-9861

Digital Object Identifier (DOI)

  • 10.1016/0003-9861(83)90385-5


  • eng

Conference Location

  • United States