Cross-linking and proteolysis in Ca2+-treated lens homogenates
- 31 August 1990
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1040 (2) , 187-191
- https://doi.org/10.1016/0167-4838(90)90074-p
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Chicken skeletal muscle has three Ca2+-dependent proteinasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- INHIBITION OF BETA-CRYSTALLIN CROSS-LINKING IN THE CA-2+-TREATED LENS1987
- Inhibition of protein cross-linking in calcium-enriched human erythrocytes and activated plateletsBiochemistry, 1987
- Degradation of Vimentin in a Cataract Model: The Ca2+-Treated LensAnnals of the New York Academy of Sciences, 1985
- Formation of a 55,000 molecular-weight crosslinked .beta. crystallin dimer in the calcium treated lens. A model for cataractBiochemistry, 1985
- Degradation of transmembrane proteins in Ca2+-enriched human erythrocytes. An immunochemical study.Journal of Biological Chemistry, 1983
- Specificity of guinea pig liver transglutaminase for amine substratesBiochemistry, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Amine specificity in transpeptidation. Inhibition of fibrin cross-linkingBiochemistry, 1968