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Laser desorption ionization mass spectrometry in the study of natural and synthetic melanins II—serotonin melanins
Author(s) -
Bertazzo Antonella,
Biasiolo Monica,
Costa Carlo,
Allegri Graziella,
Elli Giuseppe,
Seraglia Roberta,
Traldi Pietro
Publication year - 1994
Publication title -
biological mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1052-9306
DOI - 10.1002/bms.1200230703
Subject(s) - polyphenol oxidase , chemistry , oligomer , tyrosinase , sepia , mass spectrometry , melanin , desorption , chromatography , biochemistry , officinalis , enzyme , organic chemistry , botany , biology , adsorption , peroxidase
Various biosynthetic melanins obtained by enzymic oxidation of serotonin with polyphenol oxidase from Psalliota campestris mushroom or potato, and with tyrosinase from Sepia officinalis or from Sigma were studied by means of laser desorption ionization mass spectrometry. Various oligomeric clusters were evidenced, proving that the examined melanins are composed of sets of different oligomers, the production of which strongly depends on the enzyme reaction. While serotonin melanins obtained with polyphenol oxidase from potato showed wide species distribution with molecular weights ranging from 2008 to 13000 Da, the same melanins obtained from mushroom showed oligomer distributions from 1505 to 9000 Da. Serotonin melanins prepared with tyrosinase from Sepia showed oligomers from 1636 to 18000 Da. A dopa‐melanin obtained with mushroom polyphenol oxidase showed oligomer species from 1709 to 17874 Da. Comparison of molecular weight distributions of the various oligomer sets in serotonin melanins with those in tyrosine melanins revealed clear differences, which are investigated and discussed.