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Relationship Between Tyrosinase Inhibitory Action and Oxidation-Reduction Potential of Cosmetic Whitening Ingredients and Phenol Derivatives
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  • Relationship Between Tyrosinase Inhibitory Action and Oxidation-Reduction Potential of Cosmetic Whitening Ingredients and Phenol Derivatives
  • Relationship Between Tyrosinase Inhibitory Action and Oxidation-Reduction Potential of Cosmetic Whitening Ingredients and Phenol Derivatives
저자명
Sakuma. Katsuya,Ogawa. Masayuki,Sugibayashi. Kenji,Yamada. Koh-ichi,Yamamoto. Katsumi
간행물명
Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea
권/호정보
1999년|22권 4호|pp.335-339 (5 pages)
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대한약학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

The oxidation-reduction potentials of cosmetic raw materials, showing tyrosinase inhibitory action, and phenolic compounds structurally similar to L-tyrosine were determined by cylcic voltammetry. The voltammograms obtained could be classified ito 4 patterns (patterns 1-4). Patterns 1, characterized by oxidation and reduction peaks as a pair, was observed with catechol, hydroquinone or phenol, and pattern 2 exhibiting another oxidation peak in addition to oxidation and reduction peaks as a pair was found with arbutin, kojic acid, resorcinol, methyl p-hydroxybenzoate and L-tyrosine as the substrate of tyrosinase. Pattern 3 with an independent oxidation peak only was expressed by L-ascorbic acid, and pattern 4 with a reduction peak only at high potentials, by hinokitiol. The tyrosinase inhibitory activity of these compounds was also evaluated using the 50% inhibitory concentration ($IC_{50}$) and the inhibition constant (Ki) as parameters. Hinokitiol, classified as patterns 4, showed the highest inhibitory activity (lowest $IC_{50}$ and Ki). Hydroquinone showing the second highest activity belonged to pattern 1, which also included compounds exhibiting pattern 2 was relatively low with Ki values being in the order of 10-4 M. Although there was no consistent relationship between oxidation-reduction potentials and tyrosinase inhibitory action, the voltammetry data can be used as an additional index to establish the relationship between the structure and the tyrosine inhibitory activity.