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- W1964018001 abstract "Using Triton X-100 solubilization and sucrose gradient fractionation, a photosystem II core complex has been isolated from the green alga Dunaliella salina. The complex was similar to that previously isolated from spinach [(1985) FEBS Lett. 188, 68-72] being composed of five main polypeptides of apparent molecular masses, 47, 40, 32, 30 and 10 kDa. Studies using 14C indicate that with either dark or illuminated cells the Stoichiometry of these polypeptides is 1:1:1:1:1 with about 20 chlorophyll a molecules per monomeric unit. According to 35S labelling only the 32 kDa polypeptide, identified as the D1 or QB binding protein by immunoblotting, is rapidly turning over at a rate greater than the growth rate. The level of labelled sulphur associated with each polypeptide is reasonably consistent with the amino acid content derived from gene sequences and identifies the 47, 40, 32, 30 and 10 kDa apoproteins as products of the psbB, psbC, psbA, psbD and psbE genes." @default.
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- W1964018001 date "1987-01-19" @default.
- W1964018001 modified "2023-09-25" @default.
- W1964018001 title "Stoichiometry and turnover of photosystem II polypeptides" @default.
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- W1964018001 doi "https://doi.org/10.1016/0014-5793(87)81281-4" @default.
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