Kinetic analyses of two-steps oxidation from l-tyrosine to l-dopaquinone with tyrosinase by capillary electrophoresis/dynamic frontal analysis
Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from l-tyrosine to l-dopa or from l-dopa to l-dopaquinone. In thi...
Saved in:
| Published in | Analytical biochemistry Vol. 655; p. 114856 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Elsevier Inc
15.10.2022
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from l-tyrosine to l-dopa or from l-dopa to l-dopaquinone. In this study, kinetic analyses of two-steps oxidation of l-tyrosine with tyrosinase were made by capillary electrophoresis/dynamic frontal analysis (CE/DFA). When l-dopa was introduced into a capillary as a sample plug in a CE/DFA format, the enzymatic oxidation continuously occurred during the electrophoresis, and the product l-dopaquinone was subsequently converted to dopachrome which was detected as a plateau signal. A Michaelis-Menten constant of the second-step kinetic reaction, Km,Do, was determined as 0.45 ± 0.03 mmol L−1. In the analysis of the first-step kinetic reaction from l-tyrosine to l-dopa, l-dopa was not resolved by CE/DFA because both l-tyrosine and l-dopa are electrically neutral. The l-dopa formed and co-migrated at the l-tyrosine zone was calibrated beforehand with the final product of dopachrome detected as a plateau signal. Constantly formed l-dopa was successfully detected as a plateau signal of dopachrome, and a Michaelis-Menten constant of Km,Ty was also determined as 0.061 ± 0.009 mmol L−1 by the CE/DFA. CE/DFA is applicable to two-steps enzymatic reactions.
[Display omitted]
•Two-steps enzymatic oxidation with tyrosinase was analyzed by CE/DFA.•A final product of dopachrome was continuously resolved from the substrate zone.•Plateau signal under the enzymatic oxidation was provided for the kinetic analysis.•The two-steps reactions were independently analyzed without substrate inhibition. |
|---|---|
| AbstractList | Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from l-tyrosine to l-dopa or from l-dopa to l-dopaquinone. In this study, kinetic analyses of two-steps oxidation of l-tyrosine with tyrosinase were made by capillary electrophoresis/dynamic frontal analysis (CE/DFA). When l-dopa was introduced into a capillary as a sample plug in a CE/DFA format, the enzymatic oxidation continuously occurred during the electrophoresis, and the product l-dopaquinone was subsequently converted to dopachrome which was detected as a plateau signal. A Michaelis-Menten constant of the second-step kinetic reaction, Kₘ,Dₒ, was determined as 0.45 ± 0.03 mmol L⁻¹. In the analysis of the first-step kinetic reaction from l-tyrosine to l-dopa, l-dopa was not resolved by CE/DFA because both l-tyrosine and l-dopa are electrically neutral. The l-dopa formed and co-migrated at the l-tyrosine zone was calibrated beforehand with the final product of dopachrome detected as a plateau signal. Constantly formed l-dopa was successfully detected as a plateau signal of dopachrome, and a Michaelis-Menten constant of Kₘ,Ty was also determined as 0.061 ± 0.009 mmol L⁻¹ by the CE/DFA. CE/DFA is applicable to two-steps enzymatic reactions. Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from l-tyrosine to l-dopa or from l-dopa to l-dopaquinone. In this study, kinetic analyses of two-steps oxidation of l-tyrosine with tyrosinase were made by capillary electrophoresis/dynamic frontal analysis (CE/DFA). When l-dopa was introduced into a capillary as a sample plug in a CE/DFA format, the enzymatic oxidation continuously occurred during the electrophoresis, and the product l-dopaquinone was subsequently converted to dopachrome which was detected as a plateau signal. A Michaelis-Menten constant of the second-step kinetic reaction, Km,Do, was determined as 0.45 ± 0.03 mmol L-1. In the analysis of the first-step kinetic reaction from l-tyrosine to l-dopa, l-dopa was not resolved by CE/DFA because both l-tyrosine and l-dopa are electrically neutral. The l-dopa formed and co-migrated at the l-tyrosine zone was calibrated beforehand with the final product of dopachrome detected as a plateau signal. Constantly formed l-dopa was successfully detected as a plateau signal of dopachrome, and a Michaelis-Menten constant of Km,Ty was also determined as 0.061 ± 0.009 mmol L-1 by the CE/DFA. CE/DFA is applicable to two-steps enzymatic reactions.Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from l-tyrosine to l-dopa or from l-dopa to l-dopaquinone. In this study, kinetic analyses of two-steps oxidation of l-tyrosine with tyrosinase were made by capillary electrophoresis/dynamic frontal analysis (CE/DFA). When l-dopa was introduced into a capillary as a sample plug in a CE/DFA format, the enzymatic oxidation continuously occurred during the electrophoresis, and the product l-dopaquinone was subsequently converted to dopachrome which was detected as a plateau signal. A Michaelis-Menten constant of the second-step kinetic reaction, Km,Do, was determined as 0.45 ± 0.03 mmol L-1. In the analysis of the first-step kinetic reaction from l-tyrosine to l-dopa, l-dopa was not resolved by CE/DFA because both l-tyrosine and l-dopa are electrically neutral. The l-dopa formed and co-migrated at the l-tyrosine zone was calibrated beforehand with the final product of dopachrome detected as a plateau signal. Constantly formed l-dopa was successfully detected as a plateau signal of dopachrome, and a Michaelis-Menten constant of Km,Ty was also determined as 0.061 ± 0.009 mmol L-1 by the CE/DFA. CE/DFA is applicable to two-steps enzymatic reactions. Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from l-tyrosine to l-dopa or from l-dopa to l-dopaquinone. In this study, kinetic analyses of two-steps oxidation of l-tyrosine with tyrosinase were made by capillary electrophoresis/dynamic frontal analysis (CE/DFA). When l-dopa was introduced into a capillary as a sample plug in a CE/DFA format, the enzymatic oxidation continuously occurred during the electrophoresis, and the product l-dopaquinone was subsequently converted to dopachrome which was detected as a plateau signal. A Michaelis-Menten constant of the second-step kinetic reaction, Km,Do, was determined as 0.45 ± 0.03 mmol L−1. In the analysis of the first-step kinetic reaction from l-tyrosine to l-dopa, l-dopa was not resolved by CE/DFA because both l-tyrosine and l-dopa are electrically neutral. The l-dopa formed and co-migrated at the l-tyrosine zone was calibrated beforehand with the final product of dopachrome detected as a plateau signal. Constantly formed l-dopa was successfully detected as a plateau signal of dopachrome, and a Michaelis-Menten constant of Km,Ty was also determined as 0.061 ± 0.009 mmol L−1 by the CE/DFA. CE/DFA is applicable to two-steps enzymatic reactions. [Display omitted] •Two-steps enzymatic oxidation with tyrosinase was analyzed by CE/DFA.•A final product of dopachrome was continuously resolved from the substrate zone.•Plateau signal under the enzymatic oxidation was provided for the kinetic analysis.•The two-steps reactions were independently analyzed without substrate inhibition. |
| ArticleNumber | 114856 |
| Author | Takayanagi, Toshio Mine, Masanori Mizuguchi, Hitoshi |
| Author_xml | – sequence: 1 givenname: Masanori surname: Mine fullname: Mine, Masanori organization: Graduate School of Advanced Technology and Science, Tokushima University, 2-1 Minamijyousanjima-cho, Tokushima, 770-8506, Japan – sequence: 2 givenname: Hitoshi surname: Mizuguchi fullname: Mizuguchi, Hitoshi organization: Graduate School of Technology, Industrial and Social Sciences, Tokushima University, 2-1 Minamijyousanjima-cho, Tokushima, 770-8506, Japan – sequence: 3 givenname: Toshio orcidid: 0000-0002-5767-1126 surname: Takayanagi fullname: Takayanagi, Toshio email: toshio.takayanagi@tokushima-u.ac.jp organization: Graduate School of Technology, Industrial and Social Sciences, Tokushima University, 2-1 Minamijyousanjima-cho, Tokushima, 770-8506, Japan |
| BookMark | eNqNkT1vFDEQhi0UJC4ffUqXNHsZe3e9t3QogoCIRENqyx9jxac9e2P7CPsn8pvxcVchEVFZI7_PzOiZc3IWYkBCrhmsGTBxs10rvebA-ZqxbtOLN2TFYBQNtDCekRUAtA0X4_COnOe8BaipXqzIyzcfsHhDVVDTkjHT6Gh5jk0uONfil7eq-BioS3FHp6YsKeaK0BJrZeOsnvb-sAp99uWRnr5VRqoXatTsp0mlheKEpqQ4P8aE2ecbuwS1q1Nr11DUdJru8yV569SU8er0XpCHz59-3H5p7r_ffb39eN-YDrrSWDVw7ZwWvUHgxrBuwL53G9S6tyPTbugF8FG3w6BZ60QnBoGOc2uxhgxvL8j7Y985xac95iJ3PhusywaM-yz5wDZt3wJn_xEFXoVvxCEqjlFTLeSEThpf_ugrSflJMpCHW8mtVFoebiWPt6og_AXOye-quNeQD0cEq6afHpPMxmMwaH2qrqWN_t_wb0JPsWw |
| CitedBy_id | crossref_primary_10_15583_jpchrom_2023_009 crossref_primary_10_1007_s10123_024_00627_2 crossref_primary_10_1016_j_bse_2024_104880 crossref_primary_10_3390_cosmetics11010021 crossref_primary_10_1093_bulcsj_uoae104 crossref_primary_10_1002_elps_202300152 crossref_primary_10_1016_j_ab_2022_115028 crossref_primary_10_1080_10286020_2023_2264784 crossref_primary_10_1080_15287394_2023_2275691 crossref_primary_10_1007_s11240_025_03023_4 crossref_primary_10_3390_molecules28135239 crossref_primary_10_1021_acs_analchem_4c00857 crossref_primary_10_1016_j_chroma_2023_464511 |
| Cites_doi | 10.1007/s00216-020-03110-9 10.1016/0021-9673(93)80298-M 10.1021/jf200990g 10.2116/analsci.19P471 10.1002/elps.201600367 10.1039/c3an00031a 10.1016/S0167-4838(01)00237-0 10.1016/j.talanta.2013.08.028 10.1002/jssc.200800671 10.1002/jssc.201500371 10.1016/j.colsurfb.2020.110800 10.1016/j.jpba.2010.04.005 10.1016/j.ab.2011.03.021 10.1016/j.talanta.2018.06.014 10.1016/0021-9673(92)87127-T 10.1016/j.jpba.2013.05.023 10.1016/S0378-4347(96)00244-7 10.1007/s00018-005-5054-y 10.1016/j.ab.2017.02.020 10.1016/j.talanta.2018.03.049 10.1371/journal.pone.0145483 10.1039/a701844d 10.1016/j.aca.2012.02.003 10.1016/j.febslet.2013.06.025 10.1016/0021-9673(94)80526-1 10.1246/cl.200130 10.1039/C4RA09433F 10.1111/j.1541-4337.2012.00191.x 10.1016/j.jpba.2020.113390 10.1039/D0AY01736A 10.1016/j.chroma.2017.11.003 |
| ContentType | Journal Article |
| Copyright | 2022 Elsevier Inc. Copyright © 2022 Elsevier Inc. All rights reserved. |
| Copyright_xml | – notice: 2022 Elsevier Inc. – notice: Copyright © 2022 Elsevier Inc. All rights reserved. |
| DBID | AAYXX CITATION 7X8 7S9 L.6 |
| DOI | 10.1016/j.ab.2022.114856 |
| DatabaseName | CrossRef MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitle | CrossRef MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | AGRICOLA MEDLINE - Academic |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry |
| EISSN | 1096-0309 |
| ExternalDocumentID | 10_1016_j_ab_2022_114856 S0003269722003165 |
| GroupedDBID | --- --K --M -~X .~1 0R~ 1B1 1RT 1~. 1~5 23M 4.4 457 4G. 5GY 5VS 6J9 7-5 71M 85S 8P~ 9JM 9JN AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AARLI AAXUO ABFNM ABFRF ABGSF ABMAC ABOCM ABUDA ABYKQ ACDAQ ACGFO ACNCT ACRLP ADBBV ADECG ADEZE ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AFZHZ AGHFR AGUBO AGYEJ AIEXJ AIKHN AITUG AJOXV AJSZI ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLXMC CS3 DM4 DOVZS EBS EFBJH EFLBG EO8 EO9 EP2 EP3 F5P FDB FIRID FLBIZ FNPLU FYGXN G-Q GBLVA HLW IHE J1W KOM L7B LG5 LX2 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 RNS ROL RPZ SBG SCC SDF SDG SDP SES SPC SPCBC SSK SSU SSZ T5K WH7 XPP Y6R ZA5 ZMT .55 .GJ 53G AAHBH AAQXK AATTM AAXKI AAYWO AAYXX ABDPE ABEFU ABWVN ABXDB ACKIV ACNNM ACRPL ACVFH ADCNI ADFGL ADIYS ADMUD ADNMO ADRHT ADVLN ADXHL AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRDE AGRNS AHHHB AI. AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP ASPBG AVWKF AZFZN BNPGV CAG CITATION COF EJD FA8 FEDTE FGOYB G-2 HVGLF HZ~ H~9 J5H K-O MVM R2- RIG SCB SEW SSH VH1 WUQ X7M XOL YYP ZGI ZKB ZY4 7X8 7S9 EFKBS L.6 |
| ID | FETCH-LOGICAL-c404t-da72bffb65ce02cc147e55f8ebb5d91bf756029b377b13f64676ef22ddef8ec23 |
| IEDL.DBID | .~1 |
| ISSN | 0003-2697 1096-0309 |
| IngestDate | Sun Aug 24 04:06:08 EDT 2025 Fri Jul 11 02:24:29 EDT 2025 Tue Jul 01 01:19:46 EDT 2025 Thu Apr 24 23:04:12 EDT 2025 Fri Feb 23 02:38:51 EST 2024 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | Kinetic analysis Dynamic frontal analysis Capillary electrophoresis Two-steps oxidation Tyrosinase |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c404t-da72bffb65ce02cc147e55f8ebb5d91bf756029b377b13f64676ef22ddef8ec23 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0000-0002-5767-1126 |
| OpenAccessLink | https://tokushima-u.repo.nii.ac.jp/records/2010171 |
| PQID | 2702485861 |
| PQPubID | 23479 |
| ParticipantIDs | proquest_miscellaneous_2718353021 proquest_miscellaneous_2702485861 crossref_citationtrail_10_1016_j_ab_2022_114856 crossref_primary_10_1016_j_ab_2022_114856 elsevier_sciencedirect_doi_10_1016_j_ab_2022_114856 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2022-10-15 |
| PublicationDateYYYYMMDD | 2022-10-15 |
| PublicationDate_xml | – month: 10 year: 2022 text: 2022-10-15 day: 15 |
| PublicationDecade | 2020 |
| PublicationTitle | Analytical biochemistry |
| PublicationYear | 2022 |
| Publisher | Elsevier Inc |
| Publisher_xml | – name: Elsevier Inc |
| References | Pan, Li, Yu, Zuo, Zheng, Shi, Liu, Lin, Liang, Wang, Chen (bib3) 2011; 59 Iqbal, Iqbal, Müller (bib17) 2013; 138 Sun, Qi, Mu, Qiao, Wang (bib25) 2013; 116 Liu, Yang, Ha, Chen, Shi (bib24) 2017; 525 Su, Mu, Qi (bib26) 2014; 4 Fayad, Morin, Nehmé (bib8) 2017; 1529 Zhang, Lu, Jiang, Wu, Zhou, Li, Yang (bib9) 2020; 188 Bao, Regnier (bib12) 1992; 608 Harmon, Patterson, Regnier (bib13) 1993; 657 Jiang, Liang, Wang, Zhang, Lv (bib21) 2013; 84 Chai, Wang, Wei, Zou, Deng, Liu, Peng (bib4) 2015; 10 Bao, Fujima, Danielson (bib10) 1997; 699 Mine, Matsumoto, Mizuguchi, Takayanagi (bib29) 2020; 12 Schäuble, Stavrum, Puntervoll, Schuster, Heiland (bib33) 2013; 587 Li, Yang, Wang, Wu, Xia, Chen (bib18) 2018; 185 Saruno, Kato, Ikeno (bib1) 1979; 43 Nehme, Nehme, Lafite, Routier, Morin (bib15) 2012; 722 Tang, Zhang, Zhao, Chen (bib23) 2015; 38 Rodríguez-López, Fenoll, Peñalver, García-Ruiz, Varón, Martínez-Ortíz, Garcı́a-Cánovas, Tudela (bib2) 2001; 1548 Krylova, Okhonin, Krylov (bib19) 2009; 32 Mine, Mizuguchi, Takayanagi (bib31) 2021; 413 Patterson, Harmon, Regnier (bib14) 1994; 662 Iqbal (bib16) 2011; 414 Kim, Uyama (bib6) 2005; 62 Mine, Mizuguchi, Takayanagi (bib30) 2020; 188 Farcaş, Pochet, Fillet (bib20) 2018; 188 Mine, Mizuguchi, Takayanagi (bib28) 2020; 49 Loizzo, Tundis, Menichini (bib5) 2012; 11 Cheng, Chen (bib22) 2017; 38 Fan, Scriba (bib11) 2010; 53 Robinson, Smyth (bib7) 1997; 122 Takayanagi, Mine, Mizuguchi (bib27) 2020; 36 The R Project for Statistical Computing. https://www.r-project.org/(accessed 9 April 2022). Nehme (10.1016/j.ab.2022.114856_bib15) 2012; 722 Loizzo (10.1016/j.ab.2022.114856_bib5) 2012; 11 Iqbal (10.1016/j.ab.2022.114856_bib16) 2011; 414 Iqbal (10.1016/j.ab.2022.114856_bib17) 2013; 138 Rodríguez-López (10.1016/j.ab.2022.114856_bib2) 2001; 1548 Bao (10.1016/j.ab.2022.114856_bib10) 1997; 699 Mine (10.1016/j.ab.2022.114856_bib28) 2020; 49 Mine (10.1016/j.ab.2022.114856_bib30) 2020; 188 Zhang (10.1016/j.ab.2022.114856_bib9) 2020; 188 Pan (10.1016/j.ab.2022.114856_bib3) 2011; 59 Bao (10.1016/j.ab.2022.114856_bib12) 1992; 608 Fayad (10.1016/j.ab.2022.114856_bib8) 2017; 1529 Takayanagi (10.1016/j.ab.2022.114856_bib27) 2020; 36 10.1016/j.ab.2022.114856_bib32 Patterson (10.1016/j.ab.2022.114856_bib14) 1994; 662 Jiang (10.1016/j.ab.2022.114856_bib21) 2013; 84 Kim (10.1016/j.ab.2022.114856_bib6) 2005; 62 Fan (10.1016/j.ab.2022.114856_bib11) 2010; 53 Liu (10.1016/j.ab.2022.114856_bib24) 2017; 525 Sun (10.1016/j.ab.2022.114856_bib25) 2013; 116 Robinson (10.1016/j.ab.2022.114856_bib7) 1997; 122 Krylova (10.1016/j.ab.2022.114856_bib19) 2009; 32 Mine (10.1016/j.ab.2022.114856_bib29) 2020; 12 Li (10.1016/j.ab.2022.114856_bib18) 2018; 185 Tang (10.1016/j.ab.2022.114856_bib23) 2015; 38 Farcaş (10.1016/j.ab.2022.114856_bib20) 2018; 188 Su (10.1016/j.ab.2022.114856_bib26) 2014; 4 Saruno (10.1016/j.ab.2022.114856_bib1) 1979; 43 Cheng (10.1016/j.ab.2022.114856_bib22) 2017; 38 Mine (10.1016/j.ab.2022.114856_bib31) 2021; 413 Harmon (10.1016/j.ab.2022.114856_bib13) 1993; 657 Schäuble (10.1016/j.ab.2022.114856_bib33) 2013; 587 Chai (10.1016/j.ab.2022.114856_bib4) 2015; 10 |
| References_xml | – volume: 62 start-page: 1707 year: 2005 end-page: 1723 ident: bib6 article-title: Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future publication-title: Cell. Mol. Life Sci. – volume: 138 start-page: 3104 year: 2013 end-page: 3116 ident: bib17 article-title: Advances in immobilized enzyme microbioreactors in capillary electrophoresis publication-title: Analyst – volume: 53 start-page: 1076 year: 2010 end-page: 1090 ident: bib11 article-title: Advances in-capillary electrophoretic enzyme assays publication-title: J. Pharm. Biomed. Anal. – volume: 185 start-page: 16 year: 2018 end-page: 22 ident: bib18 article-title: Evaluation of thrombin inhibitory activity of catechins by online capillary electrophoresis-based immobilized enzyme microreactor and molecular docking publication-title: Talanta – volume: 188 start-page: 516 year: 2018 end-page: 521 ident: bib20 article-title: Transverse diffusion of laminar flow profiles as a generic capillary electrophoresis method for in-line nanoreactor mixing: application to the investigation of antithrombotic activity publication-title: Talanta – volume: 722 start-page: 127 year: 2012 end-page: 135 ident: bib15 article-title: New development in in-capillary electrophoresis techniques for kinetic and inhibition study of enzymes publication-title: Anal. Chim. Acta – reference: The R Project for Statistical Computing. https://www.r-project.org/(accessed 9 April 2022). – volume: 662 start-page: 389 year: 1994 end-page: 395 ident: bib14 article-title: Electrophoretically mediated microanalysis of calcium publication-title: J. Chromatogr. A – volume: 608 start-page: 217 year: 1992 end-page: 224 ident: bib12 article-title: Ultramicro enzyme assays in a capillary electrophoretic system publication-title: J. Chromatogr. A – volume: 12 start-page: 5846 year: 2020 end-page: 5851 ident: bib29 article-title: Kinetic analysis of an enzymatic hydrolysis of publication-title: Anal. Methods – volume: 413 start-page: 1453 year: 2021 end-page: 1460 ident: bib31 article-title: Kinetic analysis of the transphosphorylation with creatine kinase by pressure-assisted capillary electrophoresis/dynamic frontal analysis publication-title: Anal. Bioanal. Chem. – volume: 414 start-page: 226 year: 2011 end-page: 231 ident: bib16 article-title: An enzyme immobilized microassay in capillary electrophoresis for characterization and inhibition studies of alkaline phosphatases publication-title: Anal. Biochem. – volume: 699 start-page: 481 year: 1997 end-page: 497 ident: bib10 article-title: Determination of minute enzymatic activities by means of capillary electrophoretic techniques publication-title: J. Chromatogr. B – volume: 657 start-page: 429 year: 1993 end-page: 434 ident: bib13 article-title: Electrophoretically mediated microanalysis of ethanol publication-title: J. Chromatogr. A – volume: 38 start-page: 2887 year: 2015 end-page: 2892 ident: bib23 article-title: Tyrosinase inhibitor screening in traditional Chinese medicines by electrophoretically mediated microanalysis publication-title: J. Separ. Sci. – volume: 36 start-page: 829 year: 2020 end-page: 834 ident: bib27 article-title: Capillary electrophoresis/dynamic frontal analysis for the enzyme assay of 4-nitrophenyl phosphate with alkaline phosphatase publication-title: Anal. Sci. – volume: 116 start-page: 1121 year: 2013 end-page: 1125 ident: bib25 article-title: A chiral ligand exchange CE system for monitoring inhibitory effect of kojic acid on tyrosinase publication-title: Talanta – volume: 587 start-page: 2818 year: 2013 end-page: 2824 ident: bib33 publication-title: FEBS Lett. – volume: 4 start-page: 55280 year: 2014 end-page: 55285 ident: bib26 article-title: A new chiral ligand exchange capillary electrophoresis system based on Zn(II)-L-leucine complexes coordinating with β-cyclodextrin and its application in screening tyrosinase inhibitors publication-title: RSC Adv. – volume: 43 start-page: 1337 year: 1979 end-page: 1338 ident: bib1 article-title: Kojic acid, a tyrosinase inhibitor from publication-title: Agric. Biol. Chem. – volume: 188 year: 2020 ident: bib30 article-title: Kinetic analysis of substrate competition in enzymatic reactions with β-D-galactosidase by capillary electrophoresis/dynamic frontal analysis publication-title: J. Pharm. Biomed. Anal. – volume: 11 start-page: 378 year: 2012 end-page: 398 ident: bib5 article-title: Natural and synthetic tyrosinase inhibitors as antibrowning agents: an update publication-title: Compr. Rev. Food Sci. Food Saf. – volume: 32 start-page: 742 year: 2009 end-page: 756 ident: bib19 article-title: Transverse diffusion of laminar flow profiles - a generic method for mixing reactants in capillary microreactor publication-title: J. Separ. Sci. – volume: 84 start-page: 36 year: 2013 end-page: 40 ident: bib21 article-title: Immobilized capillary tyrosinase microreactor for inhibitor screening in natural extracts by capillary electrophoresis publication-title: J. Pharm. Biomed. Anal. – volume: 122 start-page: 797 year: 1997 end-page: 802 ident: bib7 article-title: Simultaneous determination of products and intermediates of L-dopa oxidation using capillary electrophoresis with diode-array detection publication-title: Analyst – volume: 188 year: 2020 ident: bib9 article-title: Tyrosinase-mediated dopamine polymerization modified magnetic alginate beads for dual-enzymes encapsulation: preparation, performance and application publication-title: Colloids Surf., B – volume: 38 start-page: 486 year: 2017 end-page: 493 ident: bib22 article-title: Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking publication-title: Electrophoresis – volume: 49 start-page: 681 year: 2020 end-page: 684 ident: bib28 article-title: Inhibition assay of theophylline by capillary electrophoresis/dynamic frontal analysis on the hydrolysis of publication-title: Chem. Lett. – volume: 1529 start-page: 1 year: 2017 end-page: 28 ident: bib8 article-title: Use of chromatographic and electrophoretic tools for assaying elastase, collagenase, hyaluronidase, and tyrosinase activity publication-title: J. Chromatogr. A – volume: 1548 start-page: 238 year: 2001 end-page: 256 ident: bib2 article-title: Tyrosinase action on monophenols: evidence for direct enzymatic release of publication-title: Biochim. Biophys. Acta – volume: 10 year: 2015 ident: bib4 article-title: Proanthocyanidins extracted from publication-title: PLoS One – volume: 59 start-page: 6645 year: 2011 end-page: 6649 ident: bib3 article-title: Synthesis and antityrosinase activities of alkyl 3,4-dihydroxybenzoates publication-title: J. Agric. Food Chem. – volume: 525 start-page: 54 year: 2017 end-page: 59 ident: bib24 article-title: Kinetics and inhibition study of tyrosinase by pressure mediated microanalysis publication-title: Anal. Biochem. – volume: 413 start-page: 1453 year: 2021 ident: 10.1016/j.ab.2022.114856_bib31 article-title: Kinetic analysis of the transphosphorylation with creatine kinase by pressure-assisted capillary electrophoresis/dynamic frontal analysis publication-title: Anal. Bioanal. Chem. doi: 10.1007/s00216-020-03110-9 – volume: 657 start-page: 429 year: 1993 ident: 10.1016/j.ab.2022.114856_bib13 article-title: Electrophoretically mediated microanalysis of ethanol publication-title: J. Chromatogr. A doi: 10.1016/0021-9673(93)80298-M – volume: 59 start-page: 6645 year: 2011 ident: 10.1016/j.ab.2022.114856_bib3 article-title: Synthesis and antityrosinase activities of alkyl 3,4-dihydroxybenzoates publication-title: J. Agric. Food Chem. doi: 10.1021/jf200990g – volume: 36 start-page: 829 year: 2020 ident: 10.1016/j.ab.2022.114856_bib27 article-title: Capillary electrophoresis/dynamic frontal analysis for the enzyme assay of 4-nitrophenyl phosphate with alkaline phosphatase publication-title: Anal. Sci. doi: 10.2116/analsci.19P471 – volume: 38 start-page: 486 year: 2017 ident: 10.1016/j.ab.2022.114856_bib22 article-title: Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking publication-title: Electrophoresis doi: 10.1002/elps.201600367 – volume: 43 start-page: 1337 year: 1979 ident: 10.1016/j.ab.2022.114856_bib1 article-title: Kojic acid, a tyrosinase inhibitor from Aspergillus albus publication-title: Agric. Biol. Chem. – volume: 138 start-page: 3104 year: 2013 ident: 10.1016/j.ab.2022.114856_bib17 article-title: Advances in immobilized enzyme microbioreactors in capillary electrophoresis publication-title: Analyst doi: 10.1039/c3an00031a – volume: 1548 start-page: 238 year: 2001 ident: 10.1016/j.ab.2022.114856_bib2 article-title: Tyrosinase action on monophenols: evidence for direct enzymatic release of o-diphenol publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4838(01)00237-0 – volume: 116 start-page: 1121 year: 2013 ident: 10.1016/j.ab.2022.114856_bib25 article-title: A chiral ligand exchange CE system for monitoring inhibitory effect of kojic acid on tyrosinase publication-title: Talanta doi: 10.1016/j.talanta.2013.08.028 – volume: 32 start-page: 742 year: 2009 ident: 10.1016/j.ab.2022.114856_bib19 article-title: Transverse diffusion of laminar flow profiles - a generic method for mixing reactants in capillary microreactor publication-title: J. Separ. Sci. doi: 10.1002/jssc.200800671 – volume: 38 start-page: 2887 year: 2015 ident: 10.1016/j.ab.2022.114856_bib23 article-title: Tyrosinase inhibitor screening in traditional Chinese medicines by electrophoretically mediated microanalysis publication-title: J. Separ. Sci. doi: 10.1002/jssc.201500371 – volume: 188 year: 2020 ident: 10.1016/j.ab.2022.114856_bib9 article-title: Tyrosinase-mediated dopamine polymerization modified magnetic alginate beads for dual-enzymes encapsulation: preparation, performance and application publication-title: Colloids Surf., B doi: 10.1016/j.colsurfb.2020.110800 – volume: 53 start-page: 1076 year: 2010 ident: 10.1016/j.ab.2022.114856_bib11 article-title: Advances in-capillary electrophoretic enzyme assays publication-title: J. Pharm. Biomed. Anal. doi: 10.1016/j.jpba.2010.04.005 – volume: 414 start-page: 226 year: 2011 ident: 10.1016/j.ab.2022.114856_bib16 article-title: An enzyme immobilized microassay in capillary electrophoresis for characterization and inhibition studies of alkaline phosphatases publication-title: Anal. Biochem. doi: 10.1016/j.ab.2011.03.021 – volume: 188 start-page: 516 year: 2018 ident: 10.1016/j.ab.2022.114856_bib20 article-title: Transverse diffusion of laminar flow profiles as a generic capillary electrophoresis method for in-line nanoreactor mixing: application to the investigation of antithrombotic activity publication-title: Talanta doi: 10.1016/j.talanta.2018.06.014 – volume: 608 start-page: 217 year: 1992 ident: 10.1016/j.ab.2022.114856_bib12 article-title: Ultramicro enzyme assays in a capillary electrophoretic system publication-title: J. Chromatogr. A doi: 10.1016/0021-9673(92)87127-T – ident: 10.1016/j.ab.2022.114856_bib32 – volume: 84 start-page: 36 year: 2013 ident: 10.1016/j.ab.2022.114856_bib21 article-title: Immobilized capillary tyrosinase microreactor for inhibitor screening in natural extracts by capillary electrophoresis publication-title: J. Pharm. Biomed. Anal. doi: 10.1016/j.jpba.2013.05.023 – volume: 699 start-page: 481 year: 1997 ident: 10.1016/j.ab.2022.114856_bib10 article-title: Determination of minute enzymatic activities by means of capillary electrophoretic techniques publication-title: J. Chromatogr. B doi: 10.1016/S0378-4347(96)00244-7 – volume: 62 start-page: 1707 year: 2005 ident: 10.1016/j.ab.2022.114856_bib6 article-title: Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-005-5054-y – volume: 525 start-page: 54 year: 2017 ident: 10.1016/j.ab.2022.114856_bib24 article-title: Kinetics and inhibition study of tyrosinase by pressure mediated microanalysis publication-title: Anal. Biochem. doi: 10.1016/j.ab.2017.02.020 – volume: 185 start-page: 16 year: 2018 ident: 10.1016/j.ab.2022.114856_bib18 article-title: Evaluation of thrombin inhibitory activity of catechins by online capillary electrophoresis-based immobilized enzyme microreactor and molecular docking publication-title: Talanta doi: 10.1016/j.talanta.2018.03.049 – volume: 10 year: 2015 ident: 10.1016/j.ab.2022.114856_bib4 article-title: Proanthocyanidins extracted from Rhododendron pulchrum leaves as source of tyrosinase inhibitors: structure, activity, and mechanism publication-title: PLoS One doi: 10.1371/journal.pone.0145483 – volume: 122 start-page: 797 year: 1997 ident: 10.1016/j.ab.2022.114856_bib7 article-title: Simultaneous determination of products and intermediates of L-dopa oxidation using capillary electrophoresis with diode-array detection publication-title: Analyst doi: 10.1039/a701844d – volume: 722 start-page: 127 year: 2012 ident: 10.1016/j.ab.2022.114856_bib15 article-title: New development in in-capillary electrophoresis techniques for kinetic and inhibition study of enzymes publication-title: Anal. Chim. Acta doi: 10.1016/j.aca.2012.02.003 – volume: 587 start-page: 2818 year: 2013 ident: 10.1016/j.ab.2022.114856_bib33 publication-title: FEBS Lett. doi: 10.1016/j.febslet.2013.06.025 – volume: 662 start-page: 389 year: 1994 ident: 10.1016/j.ab.2022.114856_bib14 article-title: Electrophoretically mediated microanalysis of calcium publication-title: J. Chromatogr. A doi: 10.1016/0021-9673(94)80526-1 – volume: 49 start-page: 681 year: 2020 ident: 10.1016/j.ab.2022.114856_bib28 article-title: Inhibition assay of theophylline by capillary electrophoresis/dynamic frontal analysis on the hydrolysis of p-nitrophenyl phosphate with alkaline phosphatase publication-title: Chem. Lett. doi: 10.1246/cl.200130 – volume: 4 start-page: 55280 year: 2014 ident: 10.1016/j.ab.2022.114856_bib26 article-title: A new chiral ligand exchange capillary electrophoresis system based on Zn(II)-L-leucine complexes coordinating with β-cyclodextrin and its application in screening tyrosinase inhibitors publication-title: RSC Adv. doi: 10.1039/C4RA09433F – volume: 11 start-page: 378 year: 2012 ident: 10.1016/j.ab.2022.114856_bib5 article-title: Natural and synthetic tyrosinase inhibitors as antibrowning agents: an update publication-title: Compr. Rev. Food Sci. Food Saf. doi: 10.1111/j.1541-4337.2012.00191.x – volume: 188 year: 2020 ident: 10.1016/j.ab.2022.114856_bib30 article-title: Kinetic analysis of substrate competition in enzymatic reactions with β-D-galactosidase by capillary electrophoresis/dynamic frontal analysis publication-title: J. Pharm. Biomed. Anal. doi: 10.1016/j.jpba.2020.113390 – volume: 12 start-page: 5846 year: 2020 ident: 10.1016/j.ab.2022.114856_bib29 article-title: Kinetic analysis of an enzymatic hydrolysis of p-nitrophenyl acetate with carboxylesterase by pressure-assisted capillary electrophoresis/dynamic frontal analysis publication-title: Anal. Methods doi: 10.1039/D0AY01736A – volume: 1529 start-page: 1 year: 2017 ident: 10.1016/j.ab.2022.114856_bib8 article-title: Use of chromatographic and electrophoretic tools for assaying elastase, collagenase, hyaluronidase, and tyrosinase activity publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2017.11.003 |
| SSID | ssj0011456 |
| Score | 2.4821253 |
| Snippet | Tyrosinase catalyzes the oxidation of l-tyrosine in two stages to produce l-dopa and l-dopaquinone stepwise, and l-dopaquinone is subsequently converted to... |
| SourceID | proquest crossref elsevier |
| SourceType | Aggregation Database Enrichment Source Index Database Publisher |
| StartPage | 114856 |
| SubjectTerms | Capillary electrophoresis Dynamic frontal analysis enzyme kinetics Kinetic analysis L-dopa oxidation Two-steps oxidation Tyrosinase tyrosine |
| Title | Kinetic analyses of two-steps oxidation from l-tyrosine to l-dopaquinone with tyrosinase by capillary electrophoresis/dynamic frontal analysis |
| URI | https://dx.doi.org/10.1016/j.ab.2022.114856 https://www.proquest.com/docview/2702485861 https://www.proquest.com/docview/2718353021 |
| Volume | 655 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELaq9gAXRFsQ5VEZCSFxMLt2HDs5rlatFlb0gKjozbIdWwSVTehmBXvhJ_CbmUmcSkVoD5wiO-PY8jjzsGf8EfJKucyHWArmtK2YlDYwC3qZScXhNy9VITTmO3-4UItL-f4qv9oj8zEXBsMqk-wfZHovrVPNJM3mpK1rzPGdgu1RaoHxVVxhormUGlf521-3YR5g7vcIrkjMkDodVQ4xXtaBhygEXphbIIT1v1XTX0K61zznD8mDZDLS2TCqQ7IXVkfkeLYCd_nblr6mfRBnvzt-RO7NRwC3Y_J7CRYktKG2v3gkrGkTafejYcDYFgo_6wFPiWKKCb1m3RaGBU1o10CpAm_6-6ZeNVCBm7U0vQatR92WetsiXtHNliYgnfZLA557vZ5UA8Y9fhUzLVPv9foRuTw_-zRfsAS_wLycyo5VVgsXo1O5D1PhPZc65HksgnN5VXIXNVhLonSZ1o5nUYHIVSEKAQITiLzIHpN9HOQTQrMsB0_Tae-nUUofCs5DyCWsilgVZeVPyGSceePT3eQIkXFtxiC0r8Y6g7wyA69OyJvbFu1wL8cO2mxkprmztgyojR2tXo58N8A4PEexq9Bs1gZT-ICiUHwXDchKRGTiT_-r92fkPpZQS_L8OdnvbjbhBZg_nTvt1_cpOZi9Wy4u8Ln8-Hn5B2fvCcQ |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1fb9MwELdG9zBeEGwgBgOMhJB4sFo7dpw8VtWmjm592qS9WbFji6DRhDUV9EvwmXeXOJOYUB94jH2XWDnn_sR39yPkU2oT50MumNVFyaQsPCvALjOZcvjM8zQTGuudL5fp_Fp-vVE3e2Q21MJgWmXU_b1O77R1HBnHtzluqgprfCfge-RaYH4VT9UTso_dqdSI7E_PF_Plw2EClx2IK9IzZIinlX2aV2EhSBQCe-ZmiGL9b-v0SE93xufsOXkWvUY67Rf2guz51SE5mq4gYv6xpZ9pl8fZ_SA_JAezAcPtiPxZgBMJPLToeo_4Na0DbX_VDGTbwMXvqodUolhlQm9Zu4VlAQtta7gqIaD-ualWNQzg_1oap8HwUbulrmgQsuhuSyOWTvOthuC9Wo_LHuYe74rFlvHp1foluT47vZrNWURgYE5OZMvKQgsbgk2V8xPhHJfaKxUyb60qc26DBodJ5DbR2vIkpKB1Ux-EAJ0JRE4kr8gIF_ma0CRREGxa7dwkSOl8xrn3SsLGCGWWl-6YjIc3b1xsT44oGbdmyEP7bgprUFaml9Ux-fLA0fStOXbQJoMwzV_by4Dl2MH1cZC7AcHhUUqx8vVmbbCKDyiylO-iAXWJoEz8zX89_QM5mF9dXpiL8-XiLXmKM2g0uToho_Zu49-BN9Ta93G33wMd9grS |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Kinetic+analyses+of+two-steps+oxidation+from+l-tyrosine+to+l-dopaquinone+with+tyrosinase+by+capillary+electrophoresis%2Fdynamic+frontal+analysis&rft.jtitle=Analytical+biochemistry&rft.au=Mine%2C+Masanori&rft.au=Mizuguchi%2C+Hitoshi&rft.au=Takayanagi%2C+Toshio&rft.date=2022-10-15&rft.issn=0003-2697&rft.volume=655+p.114856-&rft_id=info:doi/10.1016%2Fj.ab.2022.114856&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0003-2697&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0003-2697&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0003-2697&client=summon |