A Simplified Purification and Some Properties of Ribulose 1,5-Diphosphate Carboxylase from Barley
AUTOR(ES)
Kleinkopf, G. E.
RESUMO
A rapid procedure was developed for purifying ribulose 1,5-diphosphate carboxylase from barley leaves. After (NH4)2SO4 fractionation, the unique sedimentation properties of the enzyme were exploited to effect a single step purification to 90% homogeneity. High speed centrifugation pelleted the enzyme with complete recovery of activity. Residual impurities were then removed by diethylaminoethyl cellulose chromatography and density gradient centrifugation. The purified protein exhibited size heterogeneity due to polymerization. The polymerization products were enzymatically active aggregates of ribulose 1,5-diphosphate carboxylase and were precipitated by an antibody specific for the enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=396563Documentos Relacionados
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