Structure-Function Relationship Studies of the Cytochrome Oxidases
Tsatsos, Panagiota Hristos
This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/84916
Description
Title
Structure-Function Relationship Studies of the Cytochrome Oxidases
Author(s)
Tsatsos, Panagiota Hristos
Issue Date
1999
Doctoral Committee Chair(s)
Gennis, Robert B.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
Finally, there is evidence of radical migration in the bovine cytochrome c oxidase. Upon formation of the P-state a band was seen by SDS-PAGE analysis that migrated faster than the carbonic anhydrase standard (molecular weight 36800). MALDI-TOF mass spectrometry analysis identified this as a single peak with a m/z of 34336.4, which is exactly twice the mass of subunit IV. It is believed that a covalent linkage of subunit IV is made.
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.
