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Photosystem II complexes were prepared from chloroplasts of wild type tobacco Nicotiana tabacum var. John William’s Broadleaf and from two chlorophyll mutants derived from it, namely N. tabacum Su/su and N. tabacum Su/su var. Aurea. The hydrophobic peptides of these complexes were analyzed for bound lipid molecules by means of monospecific lipid antisera. A comparison of the peptide composition of the complexes of the three chloroplast types by means of polyacrylamide gel electrophoresis showed that the peptide composition was qualitatively identical. A major quantitative difference referred to a 66 kDa peptide which appeared to be much stronger in gels of photosystem II peptides originating from the yellowgreen and the yellow tobacco variety. Furthermore, we were able to show that different SDS polyacrylamide gel electrophoresis runs of the same PS II preparation yielded differences in the band strength of this peptide. Comparative densitometric measurements showed that an increase in this 66 kDa peptide was always correlated with a decrease in the D 1  and D 2  peptides. Obviously, the 66 kDa peptide is the heterodimer of D 1  and D 2 . Differences in the peptide composition of photosystem II preparations from the 3 tobacco species refer above all to peptides of the light-harvesting complex with molecular masses of 28 and 26 kDa.

zeitschrift für naturforschung c

Binding of Lipids onto Polypeptides of the Thylakoid Membrane I. Galactolipids and Sulpholipid as Prosthetic Groups of Core Peptides of the Photosystem II Complex