Selective solubilization of chlorosome proteins in Chloroflexus aurantiacus

Citations of this article
Mendeley users who have this article in their library.


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. © 1990.




Eckhardt, A., Brunisholz, R., Frank, G., & Zuber, H. (1990). Selective solubilization of chlorosome proteins in Chloroflexus aurantiacus. FEBS Letters, 267(2), 199–202.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free