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Effects of phospholipase A 2 and alkaline pH on photosystem II particles isolated from spinach chloroplasts
Author(s) -
Tuquet Christiane,
GuillotSalomon Thérèse,
Farineau Nicole
Publication year - 1986
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1986.tb05066.x
Subject(s) - spinach , spinacia , photosystem ii , phosphatidylglycerol , tricine , phosphatidylcholine , chenopodiaceae , chloroplast , thylakoid , chemistry , biochemistry , phospholipase , photosystem i , photosystem , biophysics , chromatography , phospholipid , biology , enzyme , photosynthesis , membrane , gene
An O 2 ‐evolving photosystem II fraction (PS II particles) isolated from spinach ( Spinacia oleracea L.) chloroplasts by Triton X‐100 was treated by phospholipase A 2 or by an alkaline pH. Phospholipase A 2 depleted the particles of all phosphatidylcholine and of a part of phosphatidylglycerol containing trans ‐hexadecenoic acid, and induced a parallel inactivation of the PS II activity. The protein pattern remained similar to that of the control particles. The addition of exogenous polar lipids from thylakoids could not reactivate PS II activity. Treatment of PS II particles by an alkaline pH, known to release the 33, 24 and 18 kdalton polypeptides and to inactivate PS II activity, did not affect the lipid composition. The involvement of lipids in PS II activity is discussed.