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PMID: 9534176 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Lens alpha-crystallin: chaperone-like properties.

Methods in enzymology ·Vol. 290 ·1998-00-00 ·Pages 365-83

Horwitz J, Huang QL, Ding L, Bova MP

Abstract

暂无摘要

MeSH Terms
Alcohol Dehydrogenase/metabolism Animals Cattle Circular Dichroism Cloning, Molecular Crystallins/chemistry,metabolism Disulfides/metabolism Heat-Shock Proteins/chemistry Insulin/metabolism Lactalbumin/metabolism Molecular Chaperones/chemistry,metabolism Protein Binding/physiology Protein Denaturation Protein Folding Recombinant Proteins/chemistry
Chemicals
Crystallins Disulfides Heat-Shock Proteins Insulin Molecular Chaperones Recombinant Proteins Lactalbumin Alcohol Dehydrogenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Horwitz J
Jules Stein Eye Institute, University of California at Los Angeles School of Medicine 90095-7008, USA.
Huang Q L
Ding L
Bova M P
Article Info
Journal
Methods in enzymology
Abbr.
Methods Enzymol
ISSN
0076-6879
DOI
10.1016/s0076-6879(98)90032-5
Published
1998-00-00
Pages
365-83
Language
English
Region
United States
NLM ID
0212271
Subset
IM
Grants
NEI NIH HHS · R37-EY03897 · United States
External Links
PubMed source DOI: 10.1016/s0076-6879(98)90032-5 View journal details
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