Immunological properties of sedoheptulose-1,7-bisphosphatase from Chlamydomonas sp. W80.
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.
Tamoi
Masahiro
M
Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nara 631-8505, Japan. tamoi@nara.kindai.ac.jp
Nagaoka
Miki
M
Shigeoka
Shigeru
S
D000818:Animals; D000918:Antibody Specificity; D017360:Arabidopsis / Q000201:enzymology / Q000276:immunology; D015153:Blotting, Western; D002696:Chlamydomonas / Q000201:enzymology* / Q000235:genetics / Q000276:immunology; D003429:Cross Reactions / Q000276:immunology; D004926:Escherichia coli / Q000235:genetics; D007106:Immune Sera / Q000276:immunology; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D013403:Sugar Phosphates / Q000235:genetics / Q000276:immunology* / Q000378:metabolism*
D007106:Immune Sera; D011993:Recombinant Fusion Proteins; D013403:Sugar Phosphates; C022079:sedoheptulose 1,7-bisphosphate