Isolation of the D1 Protein and a 28-kDa Fragment of the D2 Protein from Spinach Photosystem II Membranes

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The 32-kDa D1 protein, which contained no lysine in spinach chloroplasts, as deduced from its DNA code, was isolated by high-performance gel permeation chromatography in the presence of 0.1% SDS and 4 M urea. Three proteins of the photosystem 11 reaction center complex have a molecular mass of 30-35 kDa, and two, the D2 protein and the peripheral 33-kDa protein, were severed into peptide fragments by Achromobacter lysyl endopeptidase (EC 3.4.14.50) before the chromatography. The isolated D1 protein did not contain chlorophylls and pheophytins but had an absorption maximum at 265 nm probably due to bound plastoquinone. A peptide fragment of 28 kDa from the D2 protein was also isolated from spinach photosystem II membranes and the wheat photosystem II reaction center. Antibodies raised against the 28-kDa peptide from wheat bound to the 34-kDa D2 protein, which suggested that this peptide was the largest sequence of Asp14-Lys265. The fragment of wheat D2 protein showed absorption maxima at 413 and 682 nm attributable to bound pheophytin that probably had been converted from chlorophyll a during the isolation process.
日本植物生理学会の論文