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. 1985 Jan;77(1):109–112. doi: 10.1104/pp.77.1.109

Purification and Characterization of Extracellular Pectinesterases from Phytophthora infestans

Helga Förster 1, Ihab Rasched 1
PMCID: PMC1064466  PMID: 16663990

Abstract

Constitutively produced extracellular pectinesterases from culture filtrates of the potato late blight fungus Phytophthora infestans were purified and characterized. One enzyme (PE II) was purified to homogeneity. Sodium dodecyl sulfate electrophoresis of the second enzyme (PE I) revealed two protein bands; there are indications that both proteins are pectinesterases, which were not separable by a number of different techniques. Thus, P. infestans might produce three pectinesterases in vitro. Enzyme activities were optimal in the neutral pH range and were largely dependent on the presence of NaCl or CaCl2 in the reaction medium. The molecular weight of the PE I-complex was between 45 and 48 kilodaltons, and the one of PE II was between 35 and 40 kilodaltons. Further investigations will help us to clarify the role of these enzymes during pathogenesis.

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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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