Abstract
Light harvesting (LH) bacteriochlorophyll (Bchl) protein complexes were isolated from chromatophores of Chromatium vinosum, by the combination of detergent solubilization, sodium dodecylsulfate (SDS) polyacrylamide gel electrophoresis (PAGE) and hydroxyapatite chromatography. Addition of the absorption spectra of these complexes reproduced the absorption spectrum of chromatophores from which these complexes were derived. This result led to the conclusion that these isolated complexes retained the near-infrared absorption spectra which these complexes showed as they existed in chromatophores. Two kinds of spectrally different chromatophores were obtained under different culture conditions. One of them contained two kinds of LH Bchl protein complexes; B890 containing and B850-B800 containing complexes, and the other contained, in addition, B820-B800 containing complex. B890 containing complexes from the two types of chromatophores were spectrally similar, whereas B850-B800 containing complexes were not the same with respect to the location of absorption maxima and the content of B850. It was shown that the variation of the near-infrared absorption spectra of the chromatophores is due to not only the variation of the ratio of complexes but also the variation of the absorption spectrum of a particular complex.
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