Cytoplasmic fructose-l,6-bisphosphatase (FBPase) from pea leaves was purified and characterized. The purified enzyme appeared to be homogeneous with a monomeric molecular weight of 37,000 as determined by SDS polyacrylamide gel electrophoresis. The purified enzyme was active at neutrnl pH (pH 6.0 to pH 7.0) and insensitive to dithiothreitol, as are other gluconeogenic FBPases from mammals and yeast. It was relatively stable against heat. The activation energy (Ea) and the Arrhenius frequency factor of the enzyme catalyzed reaction were 8.75 ㎉/㏖ and 1.8×10⁴/s, respectively.