6533b85efe1ef96bd12bf30f

RESEARCH PRODUCT

Messenger RNA of the large subunit of ribulose-1,5-bisphosphate carboxylase from Chlamydomonas reinhardi. Isolation and properties.

Hiroshi SanoEberhard SpaethWilliam Burton

subject

Messenger RNARibulose 15-bisphosphateImmunoprecipitationCarboxy-LyasesProtein subunitRibulose-Bisphosphate CarboxylaseChlamydomonasChlamydomonasBiologybiology.organism_classificationBiochemistryMolecular biologyPyruvate carboxylaseMolecular Weightchemistry.chemical_compoundBiochemistrychemistryPolysomePolyribosomesProtein BiosynthesisAgarose gel electrophoresisEscherichia coliRNA Messenger

description

Polysomes specifically synthesizing the large subunit of ribulose-1,5-bisphosphate carboxylase were isolated from Chlamydomonas reinhardi cells by the indirect immunoprecipitation method. Electrophoretic analysis showed that the immunoprecipitated polysomes were of chloroplast origin. The mRNA coding for the large subunit which was purified from immunoprecipitated polysomes migrated at the 19-S position on sucrose density gradients, and its molecular weight was estimated to be 7.3 x 10(5) by acid-urea/agarose gel electrophoresis. The mRNA was translated in vivo with a cell-free protein-synthesizing system derived from Escherichia coli to give full-length large-subunit polypeptides.

10.1111/j.1432-1033.1979.tb12808.xhttps://pubmed.ncbi.nlm.nih.gov/374073