Abstract
Cotton (Gossypium hirsutum L.) ovule cultures secreted a soluble peroxidase into the surrounding medium, resulting in a 200-fold increase in this activity during the 30-day growth period. The peroxidase activity was thermostable from 4°C to 60°C and displayed a pH optimum of 5.5 to 6.0. The ovule peroxidase was susceptible to periodate treatment and very resistant to protease digestion. The data suggest that the peroxidase activity is a glycoprotein. Interpretation of peroxidase data may be complicated by the presence of phenol oxidase activity in the same preparations. The presence of phenol oxidases was ruled out by the inaction of a tyrosinase-specific inhibitor, tropolone.
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Abbreviations
- PMSF:
-
phenylmethylsulfonyl fluoride
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Communicated by I.K. Vasil
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Mellon, J.E. Some characteristics of peroxidase secreted by cotton ovule cultures. Plant Cell Reports 5, 338–341 (1986). https://doi.org/10.1007/BF00268596
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DOI: https://doi.org/10.1007/BF00268596