완두잎으로부터 엽록체 fructose-1,6-bisphosphatase를 분리하여 특성에 관하여 연구하였다. 분리한 효소의 monomer 분자량은 SDS polyacrylamide gel electrophoresis 상에서 약 48,000으로 계산되었다. Sephadex G-200 gel permeation 크로마토그래피를 통해 결정된 intact 효소의 분자량은 약 160,000이었다. 그러므로 이 효소는 4개의 같은 subunit로 구성된 tetramer라고 생각된다. 이 효소는 중성 pH에서는 활성이 없었으나 알카리 pH에서는 활성을 가진다. 또한 이 효소는 $Mg^{2+}$에 의해 활성화 되었으며 dithiothreitol과 같은 환원제에 의해서도 활성화되었다. 세포질속에 있는 gluconeogenic fructose-1,6-bisphosphatase는 중성 pH에서 활성을 가지며 $Mg^{2+}$나 환원제의 영향을 받지 않는 것으로 알려져 있다. 이 효소는 세포질 fructose-1,6-bisphospha-tase의 inhibitor인 AMP에 대해 민감하지 않았다. $Mg^{2+}$에 대한 포화곡선은 S자 형태를 보이며, Hill coefficient는 3.3이었다. 효소반응의 활성화에너지$(E_a)$와 Arrhenius frequency factor (A)는 각각 21.5 kcal/mol과 $4.01{ imes}10^8/s$였으며, 활성화엔트로피$({Delta}S^{ eq0})$와 활성화엔탈피$({Delta}H^{ eq0})$는 각각 -19.7cal/$K{cdot}mol$과 20.87kcal/mol이었다.
Chloroplast fructose-1,6-bisphosphatase from pea leaves was purified and characterized. Monomeric molecular weight of the enzyme was estimated a s 48,000 by SDS polyacrylamide gel electrophoresis. Molecular weight of the intact enzyme as determined by Sephadex G-200 gel permeation chromatogrphy was about 160,000. Thus the enzyme is believed to be tetrameric and composed of four identical subunits. The purified chloroplast enzyme was inactive at neutral pH but active at alkaline pH. The enzyme was also activated by $Mg^{2+}$ and reducing agents such as dithiothreitol. Gluconeogenic fructose-1,6-bisphosphatase in cytosol is known to be active at neutral pH and insensitive to $Mg^{2+}$ and reducing agents. The enzyme was insensitive to AMP which is a potent inhibitor for cytoplasmic fructose-1,6-bis-phosphatase. The saturation curve of $Mg^{2+}$ shows sigmoidal shape and Hill coefficient was 3.3. Activation energy $(E_a)$ and Arrhenius frequency factor (A) of the enzyme catalyzed reaction were 21.5 kcal/mol and $4.01{ imes}10^8/s$, respectively. Activation entropy $({Delta}S^{ eq0})$ and activation enthalpy $({Delta}H^{ eq0})$ of the enzyme reaction were -19.17 cal/$K{cdot}mol$ and 20.87 kcal/mol, respectively.
