Abstract
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 ultrafiltered samples was left to react under an oxygen stream for 24 hours prior to lyophilization. All the samples were analyzed by matrix-assisted laser desorption/ionization mass spectrometry. The formation of protonated tetramers was observed for samples immediately lyophilized, while further non-enzymatic reaction with bubbling oxygen led to formation of larger oligomers up to octamers. Clear analogies were observed between the data obtained on the enzymatic reaction and those reported in the literature on the electrochemically induced oxidation of 5-hydroxytryptamine. © 1997 John Wiley & Sons, Ltd.
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