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. 1985 Aug;78(4):730–733. doi: 10.1104/pp.78.4.730

Isolation and Partial Purification of Prophenoloxidase from Daucus carota L. Cell Cultures 1

Kenneth Söderhäll 1, Irene Carlberg 1, Tage Eriksson 1
PMCID: PMC1064812  PMID: 16664316

Abstract

The enzyme, phenoloxidase, was isolated and partially purified as an inactive enzyme, a proenzyme, from plant cell cultures of Daucus carota, Nicotiana tabacum, and Haplopappus gracilis. The prophenoloxidase was found to be specifically activated by Ca2+ or Mn2+ ions in concentrations above 1 millimolar. Calmodulin was not involved in this activation. Concentrations of Ca2+ or Mn2+ below 1 millimolar could not induce activation of the prophenoloxidase, but if trypsin was added simultaneously with Ca2+ or Mn2+ at a concentration of 1 millimolar or below, the proenzyme was converted to its active form. The inactive form of phenoloxidase was found to be a soluble enzyme, whereas after activation the enzyme aggregated, and a significant amount of the enzyme activity could become pelleted.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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