Abstract
The Rhodopseudomonas sphaeroides form II ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBPC/O) expressed in Escherichia coli has been purified to electrophoretic homogeneity by dye-ligand column chromatography. The form II RuBPC/O made in E. coli exactly co-migrates with the R. sphaeroides enzyme in sodium dodecyl sulfate polyacrylamide slab gels. Immunological identity of the recombinant protein was verified by Western immunoblot analysis using antiserum directed against form II RuBPC/O. In addition, sequence determination of the amino terminus of the cloned gene product has established that the protein produced in E. coli under lac transcriptional control is identical to the R. sphaeroides enzyme. Based on comparisons of various catalytic properties, the RuBPC/O isolated from E. coli is functionally identical to the R. sphaeroides enzyme. The E. coli form II RuBPC/O should thus serve as an excellent model for subsequent molecular manipulation of this agriculturally important protein.
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