Mushroom Tyrosinase Inhibitory Activity of Esculetin Isolated from Seeds ofEuphorbia lathyrisL
| Autor: | Yukimitsu Masamoto, Yasuaki Shimoishi, Kyoya Takahata, Yoshiyuki Murata, Mikiro Tada, Hideya Ando |
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| Rok vydání: | 2003 |
| Předmět: |
Tyrosinase
Binding Competitive Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Levodopa Inhibitory Concentration 50 Structure-Activity Relationship chemistry.chemical_compound Column chromatography Non-competitive inhibition Coumarins Structure–activity relationship Umbelliferones Molecular Biology IC50 Euphorbia biology Silica gel Organic Chemistry Euphorbiaceae General Medicine biology.organism_classification Coumarin Kinetics chemistry Pyrones Seeds Agaricales Peptides Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 67:631-634 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.67.631 |
| Popis: | A tyrosinase inhibitor was isolated from the seeds of Euphorbia lathyris L. by bioassay-guided fractionation and purification, using silica gel column chromatography. It was identified as esculetin by comparing its physical properties and spectral data with those of an authentic sample. The IC50 value of esculetin in the mushroom tyrosinase activity test was 43 microM. The kinetic study indicates that esculetin exhibited competitive inhibition against the oxidation of 3-(3,4-dihydroxyphenyl)-alanine by mushroom tyrosinase. The structure-activity relationships among five esculetin analogs suggest that hydroxyl groups at the C6 and C7 positions of the coumarin skeleton played an important role in the expression of tyrosinase inhibitory activity. |
| Databáze: | OpenAIRE |
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