Immunological properties of sedoheptulose-1,7-bisphosphatase from Chlamydomonas sp. W80

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.