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pubmed-article:10405169pubmed:abstractTextCarbohydrates with reactive aldehyde and ketone groups can undergo Maillard reactions with proteins to form advanced glycation end products. Oxalate monoalkylamide was identified as one of the advanced glycation end products formed from the Maillard reaction of ascorbate with proteins. In these experiments, we have analyzed human lens proteins immunochemically for the presence of oxalate monoalkylamide. Oxalate monoalkylamide was absent in most of the very young lenses but was present in old and cataractous lenses. The highest levels were found in senile brunescent lenses. Incubation experiments using bovine lens proteins revealed that oxalate monoalkylamide could form from the ascorbate degradation products, 2,3-diketogulonate and L-threose. These data provide the first evidence for oxalate monoalkylamide in vivo and suggest that ascorbate degradation and its binding to proteins are enhanced during lens aging and cataract formation.lld:pubmed
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pubmed-article:10405169pubmed:authorpubmed-author:NagarajR HRHlld:pubmed
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pubmed-article:10405169pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:10405169pubmed:articleTitleImmunochemical detection of oxalate monoalkylamide, an ascorbate-derived Maillard reaction product in the human lens.lld:pubmed
pubmed-article:10405169pubmed:affiliationCenter for Vision Research, Department of Ophthalmology, Case Western Reserve University and University Hospitals of Cleveland, OH 44106, USA.lld:pubmed
pubmed-article:10405169pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10405169pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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