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Purification and Characterization of Pea Chloroplastic Phosphoriboisomerase

Cynthia L. Skrukrud, Ilana M. Gordon, Sally Dorwin, Xiao-Hua Yuan, Göte Johansson and Louise E. Anderson
Plant Physiology
Vol. 97, No. 2 (Oct., 1991), pp. 730-735
Stable URL: http://www.jstor.org/stable/4273895
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Purification and Characterization of Pea Chloroplastic Phosphoriboisomerase
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Abstract

Pea (Pisum sativum L.) chloroplastic phosphoriboisomerase (EC 5.3.1.6) can be purified to apparent homogeneity in less than 2 days time with a 53% yield. Important steps in the purification include heat treatment and pseudoaffinity chromatography on Red H-3BN Sepharose. The purified isomerase has a subunit molecular mass of 26.4 kD. The N-terminal sequence has been determined through 34 residues. pH optima are 7.8 (ribose-5-phosphate) and 7.7 (ribulose-5-phosphate); Km values are 0.9 millimolar (ribose-5-phosphate) and 0.6 millimolar (ribulose-5-phosphate). The enzyme is inhibited by erythrose-4-phosphate, sedoheptulosebisphosphate, glyceraldehyde-3-phosphate, and 3-phosphoglycerate at concentrations close to those found in photosynthesizing chloroplasts. Countercurrent phase partitioning experiments indicate that the pea chloroplastic phosphoriboisomerase interacts physically with phosphoribulokinase.

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