We have previously given evidence for a physical heterogeneity among proteins from photosynthetic membranes of maize chloroplast . About fifteen components have now been identified, differing in their molecular weights and also in their varying abilities to bind protochlorophyllide and chlorophyll . In this paper, we show that all these proteins have very similar amino acid compositions. A detailed chemical comparison is made between, on one hand the mixture of all proteins and on the other the smallest component of molecular weight 10 000. All the features analysed (percent of non-proteic material, partial peptide maps, N and C terminal ends and content of linked sugars) are the same in both cases. We conclude from these experiments that it is likely that all components are generated with the same basic peptide unit. This assertion seems to be confirmed by the fact that, after mild alkaline treatment all the components are converted into the smallest one, as seen by electrophoresis. Thus, within the photosynthesizing membranes, there appears to be a basic structural protein unit, present in a form that is more or less "polymerized". This may account for most of the particular, and sometimes disturbing, properties so far described for this system. It is likely that such a peptide, or a similar one, would provide a framework for all photosynthesizing structures. © 1976.
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