Glutathione inhibits the glycation and crosslinking of lens proteins by ascorbic acid
- 1 November 1988
- journal article
- research article
- Published by Elsevier in Experimental Eye Research
- Vol. 47 (5) , 737-750
- https://doi.org/10.1016/0014-4835(88)90041-3
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Ascorbic acid-induced crosslinking of lens proteins: evidence supporting a Maillard reactionBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- In vitro oxidation of ascorbic acid and its prevention by GSHBiochimica et Biophysica Acta (BBA) - General Subjects, 1987
- 3-Deoxyglucosone crosslinks proteins under physiological conditions.Agricultural and Biological Chemistry, 1987
- Aminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-LinkingScience, 1986
- Glycosylation of lens proteins in senile cataract and diabetes mellitusBiochemical and Biophysical Research Communications, 1984
- Recent Advances in Glycosylated Hemoglobin MeasurementsCRC Critical Reviews in Clinical Laboratory Sciences, 1984
- Effect of aging on the water-soluble and water-insoluble protein pattern in normal human lensExperimental Eye Research, 1982
- Glucosylation of human lens protein and cataractogenesisBiochemical and Biophysical Research Communications, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970