Abstract:When the mutant barley Mbl832C thylakoid membranes were solubilized at a lower SDS concentra-tion and subjected to discontinuous SDS-PAGE at 4 t, 4 blue-green bands were resolved. The resolved bands in order of increasing mobility were CPI, CPal, CPa2 and FC. CPI had absorption peaks at 677 nm in the red re-gion and at 438 nm in the blue region. Low temperature fluorescence emission spectrum showed that it is photo-system I reaction center complex containing less photosystem II. The spectral properties of CPal and CPa2 were similar. They had a red absorption maximum at 672 nm and a blue one at 436 nm. Their fluorescence emission peaks at 77 K were at 685 nm, indicating that they belong to photosystem II. The results in this paper indicate that the mutant barley only contains 3 chl a-protein complexes: CPI, CPal and CPa2. It totally lacks any light-harvesting chl a/b-protein complexes. Therefore, Mbl832C is a new type of chl b-less mutant and can survive independently in nature.