ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated.
If you have any questions, please contact Marianne Reed at mreed@ku.edu .
Fractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase
dc.contributor.author | Dentler, William L., Jr | |
dc.date.accessioned | 2015-03-09T20:57:18Z | |
dc.date.available | 2015-03-09T20:57:18Z | |
dc.date.issued | 1988-12-01 | |
dc.identifier.citation | Dentler, William L., Jr (1988). "Fractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase." Journal of Cell Biology, 107(6):2679-2688. http://www.dx.doi.org/10.1083/jcb.107.6.2679 | en_US |
dc.identifier.issn | 0021-9525 | |
dc.identifier.uri | http://hdl.handle.net/1808/17011 | |
dc.description | This is the publisher's version, also available electronically from http://jcb.rupress.org/content/107/6/2679. | en_US |
dc.description.abstract | Cilia were isolated from Tetrahymena thermophila, extracted with Triton X-114, and the detergent-soluble membrane + matrix proteins separated into Triton X-114 aqueous and detergent phases. The aqueous phase polypeptides include a high molecular mass polypeptide previously identified as a membrane dynein, detergent-soluble alpha and beta tubulins, and numerous polypeptides distinct from those found in axonemes. Integral membrane proteins partition into the detergent phase and include two major polypeptides of 58 and 50 kD, a 49-kD polypeptide, and 5 polypeptides in relatively minor amounts. The major detergent phase polypeptides are PAS-positive and are phosphorylated in vivo. A membrane-associated ATPase, distinct from the dynein-like protein, partitions into the Triton X-114 detergent phase and contains nearly 20% of the total ciliary ATPase activity. The ATPase requires Mg++ or Ca++ and is not inhibited by ouabain or vanadate. This procedure provides a gentle and rapid technique to separate integral membrane proteins from those that may be peripherally associated with the matrix or membrane. | en_US |
dc.publisher | Rockefeller University Press | en_US |
dc.title | Fractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase | en_US |
dc.type | Article | |
kusw.kuauthor | Dentler, William L., Jr | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1083/jcb.107.6.2679 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item does not meet KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |