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Accumulation of glycation products in α‐H pig lens crystallin and its bearing to diabetic cataract genesis
Author(s) -
Vidal P.,
CabezasCerrato J.
Publication year - 1988
Publication title -
acta ophthalmologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.534
H-Index - 87
eISSN - 1755-3768
pISSN - 1755-375X
DOI - 10.1111/j.1755-3768.1988.tb04386.x
Subject(s) - glycation , crystallin , chemistry , incubation , amadori rearrangement , chromatography , fraction (chemistry) , biochemistry , receptor
The incorporation of 14 C‐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 14 C‐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. ‐