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. 1976 Dec;58(6):773–776. doi: 10.1104/pp.58.6.773

Ribulose Diphosphate Carboxylase Synthesis in Euglena

III. Serological Relationships of the Intact Enzyme and its Subunits 1

Richard H Brown a, Terence L Armitage a, Michael J Merrett a
PMCID: PMC542306  PMID: 16659764

Abstract

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 NH2-terminal amino acid analyses provided further evidence of variability in the structure of the small subunits.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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