Accumulation of glycation products in α‐H pig lens crystallin and its bearing to diabetic cataract genesis
- 1 October 1988
- journal article
- research article
- Published by Wiley in Acta Ophthalmologica
- Vol. 66 (5) , 589-592
- https://doi.org/10.1111/j.1755-3768.1988.tb04386.x
Abstract
The incorporation of 14C‐glucose in native pig crystallin by in vitro incubation was found, after subsequent dialysis, to affect all 5 classes of crystallin separated by Sepharose CL‐6B column chromatography. Though the radioactivity of the α‐H fraction was three times greater than that of any of the others, autoradiographs of SDS‐PAGE gels showed 14C‐glucose adducts to be present in all soluble protein subunits, without there being any evidence of preferential glycation of the α‐H subunits. The concentration of stable glycation products in the α‐H Chromatographic fraction of soluble crystalline is suggested to be due the addition of glycated material to this fraction as result of glycation‐induced hyperaggregation, and not because the α‐H subunits were especially susceptible to glycation. ‐Keywords
This publication has 10 references indexed in Scilit:
- Non-enzymatic glycosylation in human diabetic lens crystallinsDiabetologia, 1986
- Nonenzymatic glycation of human lens crystallin. Effect of aging and diabetes mellitus.Journal of Clinical Investigation, 1984
- [7] Measurement of nonenzymatic protein glycosylationPublished by Elsevier ,1984
- Increased glycosylation of proteins from cataractous lenses in diabetesDiabetologia, 1983
- Effect of aging on the water-soluble and water-insoluble protein pattern in normal human lensExperimental Eye Research, 1982
- Nonenzymatic glycosylation of bovine lens crystallins. Effect of aging.Journal of Biological Chemistry, 1981
- Diabetic cataract formation: potential role of glycosylation of lens crystallins.Proceedings of the National Academy of Sciences, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- 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