Diehn S H, Burkhart W, Graham J S
Department of Biological Sciences, Bowling Green State University, OH 43403.
Biochem Biophys Res Commun. 1993 Sep 15;195(2):928-34. doi: 10.1006/bbrc.1993.2133.
We have isolated a peroxidase activity to electrophoretic homogeneity from the leaves of the soybean plant, Glycine max. The highly anionic peroxidase isozyme has an isoelectric point of 3.7 and a molecular mass of 32 kilodaltons. Partial amino acid sequence information confirms the identity of the enzyme as a peroxidase but shows significant deviation from other plant peroxidases in the distal histidine box. The enzyme is developmentally regulated as it begins to accumulate in 8-10 day old leaves and its level remains fairly constant thereafter. The expression of this isozyme is also responsive to environmental cues in that it accumulates in young (less than 8 day old) leaves as a consequence of mechanical wounding. The appearance of the isozyme begins approximately 8 hr post-wounding and continues to accumulate for 48 hr.
