Abstract
Intact isolated pea chloroplasts use light energy to incorporate labelled amino acids into protein. 25 % of this incorporation is present in a 150 000 × g chloroplast supernatant fraction. When this supernatant is analysed on sodium dodecyl sulphate polyacrylamide gels only one polypeptide is labelled. This polypeptide is the large subunit of Fraction I protein, a major protein constituent of the chloroplast. Identity of the soluble in vitro product with the large subunit of Fraction I protein was established by comparing a tryptic map of its [ 35S]methionine-labelled peptides with a tryptic map of the large subunit of Fraction I protein labelled in vivo with [ 35S]methionine. We conclude that only one of the many chloroplast soluble proteins, namely the large subunit of Fraction I protein, is synthesised on chloroplast ribosomes.
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