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Article: High-performance liquid chromatographic determination of creatine kinase activity influenced by methylglyoxal

TitleHigh-performance liquid chromatographic determination of creatine kinase activity influenced by methylglyoxal
Authors
Issue Date2009
PublisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0269-3879/
Citation
Biomedical Chromatography, 2009, v. 23 n. 2, p. 170-174 How to Cite?
AbstractProtein glycation has been implicated in the development of diabetic complications and other health disorders, which mainly arise from accumulation of advanced glycation endproducts (AGEs) in vivo. Methylglyoxal (MGO), a typical reactive intermediate carbonyl formed in early glycation process, can react non-enzymatically with N-terminal amino groups on proteins, leading to their inactivation and generation of detrimental AGEs. Recently, it was reported that activity of creatine kinase (CK, EC 2.7.3.2) could be reduced or even eliminated completely after incubation with MGO in vitro. CK activity is usually determined by conventional colorimetric assays. However, these methods are not appropriate for monitoring the influence of MGO on CK activity since MGO can also directly react with creatine, a substrate of CK. In this study, an efficient and much more accurate HPLC approach was established to investigate the effect of MGO on CK activity. Aminoguanidine was utilized to eliminate interference from the undesirable reaction between residual MGO and creatine. It was found that higher concentrations of MGO and longer incubation time for CK and MGO caused more pronounced reduction in CK activity. This HPLC method greatly facilitates acquisition of kinetic data about CK reaction and through further improvement it may be adopted to rapidly screen potential inhibitors of MGO-induced glycation. Copyright © 2008 John Wiley & Sons, Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/179131
ISSN
2015 Impact Factor: 1.729
2015 SCImago Journal Rankings: 0.572
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPeng, Xen_US
dc.contributor.authorMa, Jen_US
dc.contributor.authorCheng, KWen_US
dc.contributor.authorChen, Ben_US
dc.contributor.authorChen, Fen_US
dc.contributor.authorWang, Men_US
dc.date.accessioned2012-12-19T09:52:14Z-
dc.date.available2012-12-19T09:52:14Z-
dc.date.issued2009en_US
dc.identifier.citationBiomedical Chromatography, 2009, v. 23 n. 2, p. 170-174en_US
dc.identifier.issn0269-3879en_US
dc.identifier.urihttp://hdl.handle.net/10722/179131-
dc.description.abstractProtein glycation has been implicated in the development of diabetic complications and other health disorders, which mainly arise from accumulation of advanced glycation endproducts (AGEs) in vivo. Methylglyoxal (MGO), a typical reactive intermediate carbonyl formed in early glycation process, can react non-enzymatically with N-terminal amino groups on proteins, leading to their inactivation and generation of detrimental AGEs. Recently, it was reported that activity of creatine kinase (CK, EC 2.7.3.2) could be reduced or even eliminated completely after incubation with MGO in vitro. CK activity is usually determined by conventional colorimetric assays. However, these methods are not appropriate for monitoring the influence of MGO on CK activity since MGO can also directly react with creatine, a substrate of CK. In this study, an efficient and much more accurate HPLC approach was established to investigate the effect of MGO on CK activity. Aminoguanidine was utilized to eliminate interference from the undesirable reaction between residual MGO and creatine. It was found that higher concentrations of MGO and longer incubation time for CK and MGO caused more pronounced reduction in CK activity. This HPLC method greatly facilitates acquisition of kinetic data about CK reaction and through further improvement it may be adopted to rapidly screen potential inhibitors of MGO-induced glycation. Copyright © 2008 John Wiley & Sons, Ltd.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons Ltd. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0269-3879/en_US
dc.relation.ispartofBiomedical Chromatographyen_US
dc.rightsBiomedical Chromatography. Copyright © John Wiley & Sons Ltd.-
dc.subject.meshAdenosine Diphosphate - Analysis - Metabolismen_US
dc.subject.meshAdenosine Triphosphate - Analysis - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChromatography, High Pressure Liquid - Methodsen_US
dc.subject.meshCreatine Kinase - Metabolismen_US
dc.subject.meshData Interpretation, Statisticalen_US
dc.subject.meshGuanidines - Chemistryen_US
dc.subject.meshMuscles - Chemistryen_US
dc.subject.meshPyruvaldehyde - Pharmacologyen_US
dc.subject.meshRabbitsen_US
dc.titleHigh-performance liquid chromatographic determination of creatine kinase activity influenced by methylglyoxalen_US
dc.typeArticleen_US
dc.identifier.emailChen, F: sfchen@hku.hken_US
dc.identifier.emailWang, M: mfwang@hku.hken_US
dc.identifier.authorityChen, F=rp00672en_US
dc.identifier.authorityWang, M=rp00800en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/bmc.1099en_US
dc.identifier.pmid18816458-
dc.identifier.scopuseid_2-s2.0-65349196269en_US
dc.identifier.hkuros163911-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-65349196269&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume23en_US
dc.identifier.issue2en_US
dc.identifier.spage170en_US
dc.identifier.epage174en_US
dc.identifier.isiWOS:000262745400009-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridPeng, X=23995738500en_US
dc.identifier.scopusauthoridMa, J=9248720900en_US
dc.identifier.scopusauthoridCheng, KW=12141247000en_US
dc.identifier.scopusauthoridChen, B=22633788300en_US
dc.identifier.scopusauthoridChen, F=7404907980en_US
dc.identifier.scopusauthoridWang, M=7406691844en_US

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