A Simplified Purification and Some Properties of Ribulose 1,5-Diphosphate Carboxylase from Barley | Zendy

G. E. Kleinkopf | Zendy; R. C. Huffaker | Zendy; A. T. Matheson | Zendy

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A Simplified Purification and Some Properties of Ribulose 1,5-Diphosphate Carboxylase from Barley

Author(s) -

G. E. Kleinkopf,

R. C. Huffaker,

A. T. Matheson

Publication year - 1970

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.46.2.204

Subject(s) - pyruvate carboxylase , centrifugation , chromatography , enzyme , chemistry , biochemistry , ribulose , fractionation , ultracentrifuge , specific activity

A rapid procedure was developed for purifying ribulose 1,5-diphosphate carboxylase from barley leaves. After (NH(4))(2)SO(4) 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.

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