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Photosystem I preparations were obtained from wild type tobacco Nicotiana tabacum var. John William’s Broadleaf (JWB) and from the two chlorophyll-deficient mutants N. tabacum Su/su and N. tabacum Su/su var. Aurea. The preparations were characterized with respect to the chlorophyll a/b ratio, their photosynthetic activity and their absorption spectroscopic properties. Peptides from these preparations were analyzed by SDS polyacrylamide gel electrophoresis and transferred for the detection of bound carotenoids according to the Western blot procedure to nitrocellulose or Immobilon membranes. The PS I preparation from the wild type JWB consisted of the core and the LHCP complex. The core complex contains the two core peptides with the same apparent MW of 66 kDa and several peptides with the lesser molecular masses of 22, 20, 19, 17, 16, 10 and 9 kDa. The light-harvesting protein complex consists of 4 subunits with the molecular masses 28, 26, 25 and 24 kDa. The PS I preparations of the yellow-green mutant Su/su and of the Aurea mutant Su/su var. Aurea contain as impurity traces of the D 1  and D 2  core peptides of photosystem II and also traces of the chlorophyll-binding photosystem II peptides with the molecular masses 42 and 47 kDa.

Immunological Evidence for the Binding of β-Carotene and Xanthophylls onto Peptides of Photosystem I from Nicotiana tabacum