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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1983 Feb;80(3):683–686. doi: 10.1073/pnas.80.3.683

Procedure for rapid isolation of photosynthetic reaction centers using cytochrome c affinity chromatography

G W Brudvig 1,*, S T Worland 1, K Sauer 1,
PMCID: PMC393443  PMID: 16578765

Abstract

Horse heart cytochrome c linked to Sepharose 4B is used to purify reaction centers from Rhodopseudomonas sphaeroides R-26. This procedure allows for an initial recovery of 80-90% of the bacterial reaction centers present in chromatophore membranes. High purity reaction centers (A280/A802 < 1.30) can be obtained with a 30% recovery. Reaction centers from wild-type Rps. sphaeroides and Rps. capsulata also bind to a cytochrome c column. Cytochrome c affinity chromatography can also be used to isolate photosystem I complexes from spinach chloroplasts.

Keywords: photosynthetic bacteria, spinach chloroplast, membrane protein purification, detergent solubilization

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Selected References

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