In Vitro Protein Synthesis by Plastids of Phaseolus vulgaris: V. Incorporation of 14C-Leucine into a Protein Fraction Containing Ribulose 1,5-Diphosphate Carboxylase 1

AUTOR(ES)

Margulies, Maurice M.

RESUMO

A crude chloroplast preparation of primary leaves of Phaseolus vulgaris was allowed to incorporate 14C-leucine into protein. A chloroplast extract was prepared and purified for ribulose 1,5-diphosphate carboxylase by ammonium sulfate precipitation, chromatography on Sephadex G-200, and chromatography on Sepharose 4B. The distribution of radioactive protein and enzyme in fractions eluted from Sepharose 4B was nearly the same. The radioactivity in the product was in peptide linkage, since it was digested to a trichloroacetic acid-soluble product by Pronase. Whole cells in the plastid preparation were not involved in the incorporation of amino acid into the fraction containing ribulose 1,5-diphosphate carboxylase, since incorporation still occurred after removal of cells. The incorporation into the fraction containing ribulose 1,5-diphosphate carboxylase occurs on ribosomes of plastids, since this incorporation is inhibited by chloramphenicol. These plastid preparations may be incorporating amino acid into ribulose 1,5-diphosphate carboxylase, but the results are not conclusive on this point.

Documentos Relacionados

• Incorporation of 14C-Leucine into Apple Leaf Protein and Its Inhibition by Protein Synthesis Inhibitors during Growth and Senescence 1
• Inhibition of Ribulose 1,5-Diphosphate Carboxylase by 6-Phosphogluconate 1
• Purification and Some Properties of Chlorella fusca Ribulose 1,5-Diphosphate Carboxylase
• Activation and Inhibition of Ribulose 1,5-Diphosphate Carboxylase by 6-Phosphogluconate 1
• Light-induced de Novo Synthesis of Ribulose 1,5-Diphosphate Carboxylase in Greening Leaves of Barley