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- Publisher Website: 10.1016/S0304-4165(03)00002-3
- Scopus: eid_2-s2.0-0037451649
- PMID: 12595094
- WOS: WOS:000181227700029
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Article: Isolation and characterization of a new advanced glycation endproduct of dehydroascorbic acid and lysine
Title | Isolation and characterization of a new advanced glycation endproduct of dehydroascorbic acid and lysine |
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Authors | |
Keywords | Chemicals And Cas Registry Numbers |
Issue Date | 2003 |
Publisher | Elsevier 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? |
Abstract | Proteins 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 Identifier | http://hdl.handle.net/10722/91074 |
ISSN | 2023 Impact Factor: 2.8 2023 SCImago Journal Rankings: 0.767 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Argirov, OK | en_HK |
dc.contributor.author | Lin, B | en_HK |
dc.contributor.author | Olesen, P | en_HK |
dc.contributor.author | Ortwerth, BJ | en_HK |
dc.date.accessioned | 2010-09-17T10:12:38Z | - |
dc.date.available | 2010-09-17T10:12:38Z | - |
dc.date.issued | 2003 | en_HK |
dc.identifier.citation | Biochimica et Biophysica Acta - General Subjects, 2003, v. 1620 n. 1-3, p. 235-244 | en_HK |
dc.identifier.issn | 0304-4165 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/91074 | - |
dc.description.abstract | Proteins 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.language | eng | en_HK |
dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbagen | en_HK |
dc.relation.ispartof | Biochimica et Biophysica Acta - General Subjects | en_HK |
dc.subject | Chemicals And Cas Registry Numbers | en_HK |
dc.title | Isolation and characterization of a new advanced glycation endproduct of dehydroascorbic acid and lysine | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Lin, B:blin@hku.hk | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/S0304-4165(03)00002-3 | en_HK |
dc.identifier.pmid | 12595094 | - |
dc.identifier.scopus | eid_2-s2.0-0037451649 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0037451649&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 1620 | en_HK |
dc.identifier.issue | 1-3 | en_HK |
dc.identifier.spage | 235 | en_HK |
dc.identifier.epage | 244 | en_HK |
dc.identifier.isi | WOS:000181227700029 | - |
dc.identifier.issnl | 0304-4165 | - |