The monomeric
chlorophyll-protein complexes, CP 29 and CP 26 seen in the Camm and Green (1980) and Dunahay and Staehelin (1986) green
gels do not always migrate in the order of the apparent molecular weight of their
apoproteins as determined by denaturing gel electrophoresis. In barley and corn they do, but in spinach they do not. In addition, in some higher plant species these
chlorophyll-protein complexes comigrate on green
gels causing
confusion in the literature. To remedy this situation and circumvent future
confusion, we propose that the CP 29 and CP 26 complexes be named according to the relative molecular weight of their
apoproteins on denaturing
gels. Our proposal is supported by the results obtained from four
antibodies used on Western blot samples of whole thylakoids, grana membranes, and PS II preparations from different plants. The higher molecular weight
proteins (proposed CP 29's) react strongly to one set of
antibodies, and the lower molecular weight
proteins (proposed CP 26's) react strongly to a different set. In spinach, CP 26
antibodies react also with CP 29, but the extent of the cross-reactivity depends critically on the gel electrophoresis system used. Accordingly, a lack of antibody reactivity under certain conditions may not indicate two
proteins are unrelated, just simply that a particular
epitope is no longer accessible following gel electrophoresis with a particular
buffer system.