Abstract
A cationic and an anionic peanut peroxidase were isolated to purity as shown by 2D electrophoresis. Amino acid analysis offered evidence for differences. Variations between the isozymes were also noted in a slight difference in the heme absorption maxima, specific enzyme activity and particularly in the relative amount of each in the suspension medium measured by the heme absorption. In contrast the two isozymes were at least partially similar in their structure as demonstrated by the crossreaction with the antisera. The percent crossreactions were used in turn to amend the calculation for the synthetic rate of each isozyme. In spite of the difference in amount secreted in the suspension medium, the in vivo biosynthetic rate of the two isozyme measured cellularly is much the same.
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Krol, C.H.M., van Huystee, R.B. Comparison of anionic with cationic peroxidase from cultured peanut cells. Plant Cell Tiss Organ Cult 22, 65–70 (1990). https://doi.org/10.1007/BF00043700
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DOI: https://doi.org/10.1007/BF00043700