Open AccessRibulose Diphosphate Carboxylase Synthesis in Euglena
Author(s) -
R. H. Brown,
Terence L. Armitage,
M. J. Merrett
Publication year - 1976
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.58.6.773
Subject(s) - euglena gracilis , euglena , biochemistry , chlorella , sodium dodecyl sulfate , biology , pyruvate carboxylase , rubisco , protein subunit , ribulose 1,5 bisphosphate , gel electrophoresis , polyacrylamide gel electrophoresis , enzyme , chloroplast , botany , algae , gene
Ribulose 1,5-diphosphate carboxylase was isolated from Euglena gracilis Klebs strain Z Pringsheim, Chlorella fusca var. vacuolata, and Chlamydobotrys stellata, and the subunits from each enzyme were separated and purified by gel filtration on Sephadex G-200 in the presence of sodium dodecyl sulfate. Rabbit antibody was elicited against purified Euglena ribulose 1,5-diphosphate carboxylase whole enzyme and the isolated large and small subunits. Euglena ribulose 1,5-diphosphate carboxylase showed partial immunological identity on Ouchterlony gels with the Chlorella and Chlamydobotrys carboxylases. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of immunoprecipitates between antibody to the Euglena large subunit and the isolated large subunits of the Chlorella and Chlamydobotrys enzymes showed this was due to determinants on the large subunit. There was no serological affinity between the small subunits of the Euglena, Chlorella, and Chlamydobotrys carboxylases, and NH(2)-terminal amino acid analyses provided further evidence of variability in the structure of the small subunits.