ISSN:
1432-0428
Keywords:
Crystallin
;
glycosylation
;
conformation
;
diabetes
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary Lens crystallins undergo non-enzymatic glycosylation with aging and diabetes mellitus. It is not known, however, whether all crystallins are subject to the same extent of glycosylation. Human diabetic lenses ( ∼80 years of age) were dissected into cortex and nucleus, then fractionated into various crystallins with gel chromatography (Sephacryl S-200, Sephdex G-75 or Bio Gel A-1 5m). The glycosylated crystallins were then separated from the nonglycosylated crystallins by affinity chromatography on Glyco Gel B boronic acid. The percentage of glycosylated crystallin was about 20–30%, and did not differ much among most crystallins, although γ-crystallin has significantly less (p 〈 0.01) glycosylated protein. The extent of glycosylation in the glycosylated crystallins, however, was found to be greater in the high molecular weight crystallins. The extent of glycosylation in α-crystallins is approximately two to four times that observed in β- or γ-crystallin. The extent of glycosylation appears to depend not only on the lysine content, which does not vary much among the crystallins, but also on the accessibility of the surface areas where lysine residues are located. This accessibility depends on the protein conformation and appears to correlate with protein unfolding.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00454880
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