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Plant and Cell Physiology, 1984, Vol. 25, No. 6 935-945
© 1984

Article

Characterization of a 47-Kilodalton Chlorophyll-Binding Polypeptide (CP-47) Isolated from a Photosystem II Core Complex

Xiao-Song Tang and Kimiyuki Satoh

Department of Biology, Faculty of Science, Okayama University Okayama 700, Japan

The purified photosystem II core complex from spinach with a particle size of about 480 kDa and containing five constituent polypeptides was further resolved by octyl-rß-D-glucopyranoside treatment followed by separation by high-performance liquid chromatography using a gel-permeation column. Of the four clearly separated, chlorophyll-containing fractions, one with a particle size of 170–180 kDa was composed entirely of a single, 47-kDa polypeptide. This chlorophyll a-polypeptide contains rß-carotene and pheophytin a, but no plastoquinone. The number of chlorophyll a associated with this polypeptide in situ was estimated to be 6–7 and an oligomeric structure of this polypeptide in vivo was proposed on the basis of its chlorophyll/protein ratio and the isolated particle size. The complex exhibited F-695 emission, but was photochemically inactive. The amino acid composition of the apoprotein was also determined.

(Received March 12, 1984; Accepted June 7, 1984)
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