Purification and partial amino acid sequence of a wound-inducible, developmentally regulated anionic peroxidase from soybean leaves.
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.
Diehn
S H
SH
Department of Biological Sciences, Bowling Green State University, OH 43403.
Burkhart
W
W
Graham
J S
JS
D000595:Amino Acid Sequence; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D006882:Hydroxyapatites; D007525:Isoelectric Focusing; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010544:Peroxidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000201:enzymology* / Q000502:physiology
D006882:Hydroxyapatites; D017886:Durapatite; D010544:Peroxidases