Purification and structural properties ofRhodospirillum rubrum ADPglucose pyrophosphorylase

ADPglucose pyrophosphorylase fromRhodospirillum rubrum has been purified to homogeneity or near homogeneity using affinity chromatography techniques. The subunit molecular weight of the enzyme is 50,000. Thus, the enzyme is similar in subunit molecular weight to that found for other bacterial ADPglucose pyrophosphorylases. The amino acid composition is similar to that found for theRhodospirillum tenue enzyme. However, the N-terminal amino acid sequence of theR. rubrum enzyme shows no apparent homology with theR. tenue enzyme N-terminal amino acid sequence.