Partial characterization of a minor chlorophyll-protein found in primary thylakoids of intermittently illuminated maize.

A mild solubilization with sodium dodecyl sulphate of intermittently illuminated maize (Zea mays L. Mvsc 429) thylakoids allows the separation of a minor chlorophyll-protein in the position of the light harvesting chlorophyll-protein monomer of green plants by polyacrylamide gel electrophoresis. It contains mainly chlorophyll a, its chlorophyll b content may come from the slightly contaminating light harvesting chlorophyll a/b-protein. It represents about 15% of the chlorophyll in protochloroplasts. The new chlorophyll-protein has an absorption maximum at 672 nm, and only one fluorescence emission peak at 680 nm. A 34 kD polypeptide is the most abundant one in the polypeptide pattern of the complex. The function of the new chlorophyll-protein is unknown at present. Its relationship to other chlorophyll-proteins is discussed.