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Two mutants of Chlorella vulgaris characterized by high (HS) or low (LS) content of sulphur‐amino acids were compared to the wild strain with respect to their protein electrophoretic pattern. Three new bands, not present in the LS and wild strains, were found in the HS mutant. In algae grown in the presence of 35S labelled sulphate two of these new bands showed a very high 35S specific activity. Some electrophoretic bands common to LS, HS, and wild strain, were present in different proportions and showed different levels of specific radioactivity for each strain. Therefore, mutational events appear to have affected both the amino acid composition of single proteins and the relative amount of proteins with high and low sulphate content. [ABSTRACT FROM AUTHOR]