IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kodama, T.
Right arrow Articles by Takemoto, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kodama, T.
Right arrow Articles by Takemoto, L.

Investigative Ophthalmology & Visual Science, Vol 29, 145-149, Copyright © 1988 by Association for Research in Vision and Ophthalmology


ARTICLES AND REPORTS

Characterization of disulfide-linked crystallins associated with human cataractous lens membranes

T Kodama and L Takemoto
Division of Biology, Kansas State University, Manhattan 66506.

In order to characterize possible disulfide-linked interactions between lens fiber cell membranes and crystallins, two-dimensional diagonal electrophoresis has been used in combination with Western blot analysis. When these blots were probed with monospecific antisera against alpha, beta and gamma crystallins, membrane from five individual normal lenses showed no disulfide-bonded components. Membrane from 13 individual cataractous human lenses showed no disulfide-bonded alpha crystallin, but did show significant amounts of disulfide-bonded beta crystallin in four out of the 13 lenses studied, and significant amounts of disulfide-bonded gamma crystallin in 10 out of the 13 lenses studied. Together, these studies demonstrate that intermolecular disulfide bonding of crystallins to purified fiber cell membranes is found only in cataractous lenses, and that the predominant polypeptide species involved in this interaction is gamma crystallin.


This article has been cited by other articles:


Home page
IOVSHome page
M. Zetterberg, X. Zhang, A. Taylor, B. Liu, J. J. Liang, and F. Shang
Glutathiolation Enhances the Degradation of {gamma}C-crystallin in Lens and Reticulocyte Lysates, Partially via the Ubiquitin-Proteasome Pathway.
Invest. Ophthalmol. Vis. Sci., August 1, 2006; 47(8): 3467 - 3473.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. B. Casey, H.-R. Zhao, and E. C. Abraham
Role of Glycine 1 and Lysine 2 in the Glycation of Bovine [IMAGE]B-Crystallin
J. Biol. Chem., September 1, 1995; 270(35): 20781 - 20786.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1988 by the Association for Research in Vision and Ophthalmology