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Ribulose Diphosphate Carboxylase Synthesis in Euglena: III. Serological Relationships of the Intact Enzyme and its Subunits.
MedLine Citation:
PMID:  16659764     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
R H Brown; T L Armitage; M J Merrett
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Plant physiology     Volume:  58     ISSN:  0032-0889     ISO Abbreviation:  Plant Physiol.     Publication Date:  1976 Dec 
Date Detail:
Created Date:  2010-06-29     Completed Date:  2010-06-29     Revised Date:  2010-09-15    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  773-6     Citation Subset:  -    
Affiliation:
Postgraduate School of Studies in Biological Sciences, University of Bradford, Bradford, Yorkshire BD7 1DP, England.
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