Inhibition Mechanism and Kinetic Model for Ozagrel on Mushroom Tyrosinase

Bai Li Shu; Ya Juan Fan; Qi Meng Zhang; Ying Li Liu; Yue Gu

doi:10.4028/www.scientific.net/AMR.236-238.2913

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HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 236-238Inhibition Mechanism and Kinetic Model for Ozagrel...

Inhibition Mechanism and Kinetic Model for Ozagrel on Mushroom Tyrosinase

Abstract:

This investigation shows that ozagrel, an antithrombotic drug, can inhibit mushroom tyrosinase well. The IC₅₀ value was 3.45 mmol/L. Ozagrel was estimated to be a reversible mixed-type inhibitor of mushroom tyrosinase by Lineweaver-Burk plots. The inhibition kinetics has been studied by using the kinetic method of the substrate reaction described by Tsou. The constants of tyrosinase and tyrosinase-substrate complex inhibited by 1.0 mmol/L ozagrel have been determined to be 87.28 and 66.07 µmol/L, respectively.

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Periodical:

Advanced Materials Research (Volumes 236-238)

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2913-2916

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.236-238.2913

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Online since:

May 2011

Authors:

Bai Li Shu, Ya Juan Fan, Qi Meng Zhang, Ying Li Liu, Yue Gu

Keywords:

Kinetic, Mushroom Tyrosinase, Ozagrel, Reversible Mix-type Inhibition

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References

[1] S.B. Li, H.L. Nie, H.T. Zhang, Y. Xue, and L.M. Zhu. Appl. Biochem. Biotechnol. Vol. 162 (2010), p.641

Google Scholar

[2] M. Schurink, W.J.H. van Berkel, H.J. Wichers, and C.G. Boeriu. Peptides. Vol. 28 (2007), p.485

DOI: 10.1016/j.peptides.2006.11.023

Google Scholar

[3] S.B. Li, Y. Xue, X.Y. Lv, H.L. Nie, L.M. Zhu, H.T. Zhang, T. Qiu, and L.M. Zhou. Protein J. Vol. 28 (2009), p.182

Google Scholar

[4] E. Selinheimo, D. NiEidhin, C. Steffensen, J. Nielsen, A. Lomascolo, S. Halaouli, E. Record, D. O'Beirne, J. Buchert, and K Kruus. J. Biotechnol. Vol. 130 (2007), p.471

DOI: 10.1016/j.jbiotec.2007.05.018

Google Scholar

[5] S.B. Li, H.L. Nie, H.T. Zhang, Y. Xue, and L.M. Zhu. Acta Phys.-Chim. Sin. Vol. 26 (2010), p.215

Google Scholar

[6] S.B. Li, Y. Xue, H.T. Zhang, H.L. Nie, and L.M. Zhu. Fine Chem. Vol. 26 (2009), p.889 (in Chinese)

Google Scholar

[7] C.L. Tsou. Adv. Enzymol. Relat. Areas Mol. Biol. Vol. 61 (1988), p.1

Google Scholar