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Selective solubilization of chlorosome proteins in Chloroflexus aurantiacus
Author(s) -
Eckhardt Anne,
Brunisholz René,
Frank Gerhard,
Zuber Herbert
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80924-8
Subject(s) - chlorosome , solubilization , chemistry , size exclusion chromatography , biochemistry , biology , bacteriochlorophyll , enzyme , photosynthesis
Proteins were solubilized selectively from chlorosomes of Chloroflexus aurantiacus by electrophoretic gel filtration according to Griebenow et al. Whereas the 11 kDa and 18 kDa proteins were extracted almost completely, the remaining modified chlorosomes contained high amounts of pigment and c‐protein. It was concluded that the c‐protein in contradiction to the publication by Griebenow et al. is indeed localized in the interior of Chloroflexus chlorosomes.