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Evidence of peroxidase activity of the peroxidation inhibiting protein on dilinoleyl phosphatidylcholine hydroperoxide as obtained in direct electron impact conditions
Author(s) -
Daolio Sergio,
Traldi Pietro,
Ursini Fulvio,
Maiorino Matilde,
Gregolin Carlo
Publication year - 1983
Publication title -
biomedical mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0306-042X
DOI - 10.1002/bms.1200100904
Subject(s) - phosphatidylcholine , chemistry , lipid peroxidation , peroxidase , fragmentation (computing) , substrate (aquarium) , enzyme , chromatography , biochemistry , membrane , phospholipid , biology , ecology
The recently purified peroxidation inhibiting protein (PIP) reduces, at the expense of glutathione oxidation, hydroperoxide groups of phospholipids. The mass spectral characterization in direct electron impact conditions of a high performance liquid chromatographic purified typical substrate of PIP (dilinoleyl phosphatidylcholine hydroperoxide) and its enzymatic reaction product is given on the basis of the fragmentation pattern of native dilinoleyl phosphatidylcholine. The results confirm the peroxidase activity of PIP and show that the direct electron impact technique is a suitable tool in mass spectrometric studies of large and thermolabile compounds as oxidation products of phospholipids.