Mass Measurements of C-terminally Truncated α-Crystallins from Two-dimensional Gels Identify Lp82 as a Major Endopeptidase in Rat Lens
Open Access
- 1 May 2002
- journal article
- Published by Elsevier in Molecular & Cellular Proteomics
- Vol. 1 (5) , 357-365
- https://doi.org/10.1074/mcp.m200007-mcp200
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Purification and Characterization of Lens Specific Calpain (Lp82) from Bovine LensExperimental Eye Research, 2001
- Protein for Lp82 Calpain Is Expressed and Enzymatically Active in Young Rat LensExperimental Eye Research, 1998
- Evidence for the involvement of calpain in cataractogenesis in Shumiya cataract rat (SCR)Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1997
- Mass Spectrometry of Whole Proteins Eluted from Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis GelsAnalytical Biochemistry, 1997
- Buthionine sulfoximine induced cataracts in mice contain insolubilized crystallins with calpain II cleavage sitesExperimental Eye Research, 1994
- Release of α-A Sequence 158-173 Correlates with a Decrease in the Molecular Chaperone Properties of Native α-CrystallinExperimental Eye Research, 1994
- Calcium Activated Proteolysis and Protein Modification in the U18666A CataractExperimental Eye Research, 1993
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- Involvement of calpain in diamide‐induced cataract in cultured lensesFEBS Letters, 1992
- Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.Proceedings of the National Academy of Sciences, 1982