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Hydrolysis of a fluorescent substance formed from an oxidized phospholipid and an amino compound by phospholipase A 2
Author(s) -
Iio Toshihiro,
Yoden Kazuaki
Publication year - 1988
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536340
Subject(s) - phospholipid , phosphatidylcholine , chemistry , phospholipase a2 , hydrolysis , fluorescence , phospholipase , liposome , biochemistry , enzyme , membrane , physics , quantum mechanics
Phosphatidylcholine hydroperoxide produced a fluorescent substance (FS‐III) through reaction with 1‐aminopentane after preincubation with heme methyl ester as a model system. The FS‐III was retained at the 2‐position of the glycerol backbone of phosphtidylcholine without breakdown into low molecular weight compounds. Phosphatidylcholine oxidized by catalysis with ferrous ion and ascorbic acid also produced the same fluorescent substance (FS‐III). Phospholipase A 2 specifically hydrolyzed the FS‐III attached to the phospholipid, making it possible to elute the same fluorescent substance (FS‐II) as that obtained from oxidized methyl linoleate. The release of FS‐II by hydrolysis of FS‐III attached to phospholipid increased with greater phospholipase A 2 activity. It is suggested that, with aging, the accumulation of fluorescent lipofuscin pigments in biomembranes may be related to changes in the peroxidized phospholipid content and that phospholipase A 2 may play a role in decreasing the formation and accumulation of fluorescent phospholipids in biomembranes.