Premium
A study of the enzymatic oligomerization of 5‐hydroxytryptamine using matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Favretto Donata,
Bertazzo Antonella,
Costa Carlo,
Allegri Graziella,
Traldi Pietro
Publication year - 1997
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19970615)11:9<1038::aid-rcm941>3.0.co;2-s
Subject(s) - chemistry , mass spectrometry , desorption , protonation , chromatography , matrix assisted laser desorption/ionization , matrix (chemical analysis) , enzyme , ionization , tyrosinase , matrix assisted laser desorption electrospray ionization , analytical chemistry (journal) , organic chemistry , adsorption , ion
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.