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Chloroplast and Cytoplasmic Enzymes

IV. Pea Leaf Fructose 1,6-Diphosphate Aldolases ^1,2

^a Department of Biological Sciences, University of Illinois at Chicago Circle, Chicago, Illinois 60680

Several peaks of aldolase activity are found in the isoelectric focusing pattern of pea (Pisum sativum) leaf chloroplast extracts. One peak, separated by 0.5 pH unit from the major chloroplast aldolase peak, is found when cytoplasmic extracts are focused. The chloroplast and cytoplasmic enzymes have a pH 7.4 optimum with fructose 1,6-diphosphate. The Michaelis constant for fructose-1,6-diphosphate is 19 µM for the chloroplast, 21 µM for the cytoplasmic enzyme, and for sedoheptulose 1,7-diphosphate, 8 µM for the chloroplast enzyme, 18 µM for the cytoplasmic enzyme. Both enzymes are inhibited by D-glyceraldehyde 3-phosphate and by ribulose 1,5-diphosphate. The similarity in the catalytic properties of the isoenzymes suggests that both enzymes have an amphibolic role in carbon metabolism in the green leaf.

² A preliminary report of these findings was presented at the II International Congress of Photosynthesis Research, Stresa, Italy, June, 1971 (4).

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