Isolation and purification of chloroplastic spinach (Spinacia oleracea) sedoheptulose-1,7-bisphosphatase.
Higher-plant sedoheptulose-1,7-bisphosphatase was isolated and purified over 200-fold from spinach (Spinacia oleracea) chloroplast stromal extracts to apparent electrophoretic homogeneity by DEAE-Fractogel, molecular sieving on Sephadex G-200 and Blue B dye-matrix affinity chromatography. It is a protein of Mr 66,000, made up of two apparently identical subunits (Mr 35,000). The enzyme is activated by reduced thioredoxin fb in the presence of dithiothreitol. Its specificity towards sedoheptulose 1,7-bisphosphate versus fructose 1,6-bisphosphate is high, but not absolute.
D054479:Chloroplast Thioredoxins; D002736:Chloroplasts / Q000201:enzymology*; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D008970:Molecular Weight; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D010940:Plant Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D013879:Thioredoxins
D054479:Chloroplast Thioredoxins; D010940:Plant Proteins; D013879:Thioredoxins; D010744:Phosphoric Monoester Hydrolases; C022627:sedoheptulose-bisphosphatase