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Article: Isolation and characterization of a new advanced glycation endproduct of dehydroascorbic acid and lysine

TitleIsolation and characterization of a new advanced glycation endproduct of dehydroascorbic acid and lysine
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2003
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbagen
Citation
Biochimica et Biophysica Acta - General Subjects, 2003, v. 1620 n. 1-3, p. 235-244 How to Cite?
AbstractProteins are subject of posttranslational modification by sugars and their degradation products in vivo. The process is often referred as glycation. L-Dehydroascorbic acid (DHA), an oxidation product of L-ascorbic acid (vitamin C), is known as a potent glycation agent. A new product of modification of lysine ε-amino group by DHA was discovered as a result of the interaction between Boc-Lys and dehydroascorbic acid. The chromatographic and spectral analyses revealed that the structure of the product was 1-(5-ammonio-5-carboxypentyl)-3-oxido-4-(hydroxymethyl)pyridinium. The same compound was isolated from DHA modified calf lens protein after hydrolysis and chromatographic separation. The study confirmed that L-erythrulose is an important intermediate of modification of proteins by DHA. The structure of the reported product and in vitro experiments suggested that L-erythrulose could further transform to L-threose, L-erythrose and glycolaldehyde under conditions similar to physiological. The present study revealed that the modification of ε-amino groups of lysine residues by DHA is a complex process and could involve a number of reactive carbonyl species. © 2003 Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91074
ISSN
2015 Impact Factor: 5.083
2015 SCImago Journal Rankings: 2.128
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorArgirov, OKen_HK
dc.contributor.authorLin, Ben_HK
dc.contributor.authorOlesen, Pen_HK
dc.contributor.authorOrtwerth, BJen_HK
dc.date.accessioned2010-09-17T10:12:38Z-
dc.date.available2010-09-17T10:12:38Z-
dc.date.issued2003en_HK
dc.identifier.citationBiochimica et Biophysica Acta - General Subjects, 2003, v. 1620 n. 1-3, p. 235-244en_HK
dc.identifier.issn0304-4165en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91074-
dc.description.abstractProteins are subject of posttranslational modification by sugars and their degradation products in vivo. The process is often referred as glycation. L-Dehydroascorbic acid (DHA), an oxidation product of L-ascorbic acid (vitamin C), is known as a potent glycation agent. A new product of modification of lysine ε-amino group by DHA was discovered as a result of the interaction between Boc-Lys and dehydroascorbic acid. The chromatographic and spectral analyses revealed that the structure of the product was 1-(5-ammonio-5-carboxypentyl)-3-oxido-4-(hydroxymethyl)pyridinium. The same compound was isolated from DHA modified calf lens protein after hydrolysis and chromatographic separation. The study confirmed that L-erythrulose is an important intermediate of modification of proteins by DHA. The structure of the reported product and in vitro experiments suggested that L-erythrulose could further transform to L-threose, L-erythrose and glycolaldehyde under conditions similar to physiological. The present study revealed that the modification of ε-amino groups of lysine residues by DHA is a complex process and could involve a number of reactive carbonyl species. © 2003 Elsevier Science B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbagenen_HK
dc.relation.ispartofBiochimica et Biophysica Acta - General Subjectsen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleIsolation and characterization of a new advanced glycation endproduct of dehydroascorbic acid and lysineen_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0304-4165(03)00002-3en_HK
dc.identifier.pmid12595094-
dc.identifier.scopuseid_2-s2.0-0037451649en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037451649&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume1620en_HK
dc.identifier.issue1-3en_HK
dc.identifier.spage235en_HK
dc.identifier.epage244en_HK
dc.identifier.isiWOS:000181227700029-

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