Polypeptide patterns obtained by polyacrylamide gel electrophoresis of thylakoid membranes isolated from light and dark grown strains of Chlorogloea fritschii.

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis has been used to determine the difference between thylakoid polypeptide patterns of light and dark grown strains of the cyanobacterium Chlorogloea fritschii. There were only 2 prominent bands present in the dark grown strains, polypeptide Mr50,000 and polypeptide Mr90,000, also five fainter bands in the Mr range 45,000-66,200 corresponding to photosystem one, compared with the 32 bands present in the light grown strains. There was no obvious indication of the Mr 33,000 3-(3,4-chlorophenyl)-1,1-dimethyl-urea binding protein. In addition the progressive daily development of the various photosystem components in the light and their relationship in photosynthesis was determined. It was observed that the increase of the relative concentrations of the photosystem two and phycocyanin components indicated their developments are mutually synchronized. The effect of light to dark and dark to light transfer on established strains was investigated. Appreciable loss of photosystem two components and the presence of an additional band Mr22,500 of unknown function in the light to dark transfer, and little reactivation of the photosynthetic capabilities in the dark to light transfer was observed.