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Updated: Aug 18, 2026

Concanavalin A-Based Sedimentation Assay to Measure Substrate Binding of Glucan Phosphatases
Published on: December 23, 2022
Immunological properties of sedoheptulose-1,7-bisphosphatase from Chlamydomonas sp. W80
Masahiro Tamoi1, Miki Nagaoka, Shigeru Shigeoka
1Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nara 631-8505, Japan. tamoi@nara.kindai.ac.jp
Abstract:
Here we report on the production of functional recombinant SBPase of Chlamydomonas sp. W80 in Escherichia coli and the one-step purification of a polyhistidine-tagged fusion protein. The polyclonal antibody was raised against purified recombinant enzyme and cross-reacted with crude SBPase from Chlamydomonas, spinach, tobacco, and Arabidopsis leaves. Further, we investigated the levels of protein and activity of SBPase in different tissues of Arabidopsis plants.
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