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- Publisher Website: 10.1002/bmc.1099
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- PMID: 18816458
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Article: High-performance liquid chromatographic determination of creatine kinase activity influenced by methylglyoxal
Title | High-performance liquid chromatographic determination of creatine kinase activity influenced by methylglyoxal |
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Authors | |
Keywords | Creatine kinase activity Glycation Ion-pair HPLC Methyglyoxal |
Issue Date | 2009 |
Publisher | John 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? |
Abstract | Protein 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 Identifier | http://hdl.handle.net/10722/179131 |
ISSN | 2023 Impact Factor: 1.8 2023 SCImago Journal Rankings: 0.384 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Peng, X | en_US |
dc.contributor.author | Ma, J | en_US |
dc.contributor.author | Cheng, KW | en_US |
dc.contributor.author | Chen, B | en_US |
dc.contributor.author | Chen, F | en_US |
dc.contributor.author | Wang, M | en_US |
dc.date.accessioned | 2012-12-19T09:52:14Z | - |
dc.date.available | 2012-12-19T09:52:14Z | - |
dc.date.issued | 2009 | en_US |
dc.identifier.citation | Biomedical Chromatography, 2009, v. 23 n. 2, p. 170-174 | en_US |
dc.identifier.issn | 0269-3879 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179131 | - |
dc.description.abstract | Protein 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.language | eng | en_US |
dc.publisher | John Wiley & Sons Ltd. The Journal's web site is located at http://www.interscience.wiley.com/jpages/0269-3879/ | en_US |
dc.relation.ispartof | Biomedical Chromatography | en_US |
dc.rights | Biomedical Chromatography. Copyright © John Wiley & Sons Ltd. | - |
dc.subject | Creatine kinase activity | - |
dc.subject | Glycation | - |
dc.subject | Ion-pair HPLC | - |
dc.subject | Methyglyoxal | - |
dc.subject.mesh | Adenosine Diphosphate - Analysis - Metabolism | en_US |
dc.subject.mesh | Adenosine Triphosphate - Analysis - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Chromatography, High Pressure Liquid - Methods | en_US |
dc.subject.mesh | Creatine Kinase - Metabolism | en_US |
dc.subject.mesh | Data Interpretation, Statistical | en_US |
dc.subject.mesh | Guanidines - Chemistry | en_US |
dc.subject.mesh | Muscles - Chemistry | en_US |
dc.subject.mesh | Pyruvaldehyde - Pharmacology | en_US |
dc.subject.mesh | Rabbits | en_US |
dc.title | High-performance liquid chromatographic determination of creatine kinase activity influenced by methylglyoxal | en_US |
dc.type | Article | en_US |
dc.identifier.email | Chen, F: sfchen@hku.hk | en_US |
dc.identifier.email | Wang, M: mfwang@hku.hk | en_US |
dc.identifier.authority | Chen, F=rp00672 | en_US |
dc.identifier.authority | Wang, M=rp00800 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1002/bmc.1099 | en_US |
dc.identifier.pmid | 18816458 | - |
dc.identifier.scopus | eid_2-s2.0-65349196269 | en_US |
dc.identifier.hkuros | 163911 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-65349196269&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 23 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 170 | en_US |
dc.identifier.epage | 174 | en_US |
dc.identifier.isi | WOS:000262745400009 | - |
dc.publisher.place | United Kingdom | en_US |
dc.identifier.scopusauthorid | Peng, X=23995738500 | en_US |
dc.identifier.scopusauthorid | Ma, J=9248720900 | en_US |
dc.identifier.scopusauthorid | Cheng, KW=12141247000 | en_US |
dc.identifier.scopusauthorid | Chen, B=22633788300 | en_US |
dc.identifier.scopusauthorid | Chen, F=7404907980 | en_US |
dc.identifier.scopusauthorid | Wang, M=7406691844 | en_US |
dc.identifier.issnl | 0269-3879 | - |