The role of tyrosinase in melanogenesis from 5-hydroxytryptamine was investigated by drawing samples from the reaction environment at different reaction times. Samples were ultrafiltered to remove the enzyme and lyophylized. In order to evaluate the role of non-enzymatic oxidation, a portion of the
A Study of the Enzymatic Oligomerization of 5,7-Dihydroxytryptamine using Matrix-assisted Laser Desorption/Ionization Mass Spectrometry
β Scribed by Antonella Bertazzo; Carlo Costa; Graziella Allegri; Donata Favretto; Pietro Traldi
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 399 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0951-4198
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β¦ Synopsis
The reaction between 5,7-dihydroxytryptne (5,7-DHT) and mushroom tyrosinase was studied by matrixassisted laser desorption/ionization mass spectrometry of various samples drawn after different reaction times (0, 30, 60, 120, 240 and 360 min), ultrafiltered and immediately lyophilized. In order to evaluate the role of nonenzymatic oxidation, a portion of the ultrafiltered sample was left to react under an oxygen stream for a further 24 hr, lyophilized and analysed by the same method. Results show that, in the case of 5,7-DHT, oligomerization products are obtained which are structurally different from those produced by the same enzymatic reaction on 5,6-DHT. This is explained by the tendency of 5,7-DHT towards oxidation, since the oligomerization products originate from oxidized forms of 5,7-DHT.
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