Summary: The pigments of were shown to exist as a carotenoprotein complex in the cell membrane and could be completely extracted by detergents. The pigments in such extracts were unstable. Sodium ascorbate (0.2%) was effective in stabilizing the pigment in the complex in Triton X-100 extracts (greater than 90% retention) and was superior to 2-mercaptoethanol, dithiothreitol, butylated hydroxytoluene, dithioerythritol and cysteine. Electrophoresis of Triton X-100 extracts in a Triton X-100-PAGE system separated the intact carotenoprotein from other membrane proteins whereas in an SDS-PAGE system the pigment was separated from the protein. All the pigments were bound to a single protein with an apparent of 15000. The protein was present in colourless and pigment mutants.


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