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PMID: 3579306 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

The nature of L8 and L8S8 forms of ribulose bisphosphate carboxylase/oxygenase from Chromatium vinosum.

Archives of biochemistry and biophysics ·Vol. 254 ·No. 1 ·1987-04-00 ·Pages 63-8

Torres-Ruiz J, McFadden BA

Abstract

L8 and L8S8 forms of ribulose bisphosphate carboxylase/oxygenase (RubisCO) have been prepared from Chromatium vinosum by the extremely mild method of centrifugal fractionation. Only the L8S8 form is detectable in crude extracts of this organism. Both forms show immunological identify in double diffusion studies using antibody to L subunits of the L8S8 form. L subunits from both L8 and L8S8 enzymes are identical by the criteria of peptides observed after limited proteolysis and N-terminal sequence analysis. In addition, these subunits show regions of homology with L subunits from Rhodospirillum rubrum, Anacystis nidulans, and spinach. S subunits of the C. vinosum enzyme are completely homologous to those from A. nidulans and higher plants from the 18th through 25th residue, a stretch preceded in all cases by two basic amino acids.

MeSH Terms
Amino Acid Sequence Chromatium/enzymology,genetics Genes, Bacterial Plants/enzymology Protein Conformation Ribulose-Bisphosphate Carboxylase/genetics,isolation & purification
Chemicals
Ribulose-Bisphosphate Carboxylase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Torres-Ruiz J
McFadden B A
Article Info
Journal
Archives of biochemistry and biophysics
Abbr.
Arch Biochem Biophys
ISSN
0003-9861
Published
1987-04-00
Pages
63-8
Language
English
Region
United States
NLM ID
0372430
Subset
IM
Grants
NIGMS NIH HHS · GM-19972 · United States
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