A homolog of ribulose bisphosphate carboxylase/oxygenase-binding protein in Chromatium vinosum.
A 700-kDa protein composed of 12 apparently identical 60-kDa subunits copurifies with the L8S8 form of ribulose bisphosphate carboxylase/oxygenase (RuBisCO) from Chromatium vinosum. Chromatography on DEAE-Sephadex A-50 separates the two proteins in pure form. On the basis of the highly reproducible copurification and reaction of the 700-kDa protein with antibodies to pea RuBisCO large (L)-subunit-binding protein, the protein from C. vinosum is designated as a putative binding protein (PBP) for RuBisCO. Also the N-terminal sequence of PBP is quite similar to that of both alpha and beta subunits of the L-subunit-binding protein. Our present research suggests that PBP may be a RuBisCO small-subunit-binding protein in C. vinosum. Measurements of RuBisCO activity and of species that immunologically cross react with RuBisCO or PBP (by enzyme-linked immunosorbent assay) establish that levels of the two proteins vary together in C. vinosum grown on different carbon sources.
Torres-Ruiz
J A
JA
Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.
McFadden
B A
BA
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002844:Chromatium / Q000201:enzymology*; D004797:Enzyme-Linked Immunosorbent Assay; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011489:Protein Denaturation; D012273:Ribulose-Bisphosphate Carboxylase / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid
D002352:Carrier Proteins; D046911:Macromolecular Substances; D012273:Ribulose-Bisphosphate Carboxylase