Abstract
Pel E, one of the four major pectate lyases produced by Erwinia chrysanthemi (Echr) strain EC16, was purified to homogeneity and was found to have an apparent molecular weight of 47 500 and a pI of 10. Antibodies produced against this preparation inhibited Pel E activity, but did not affect Pel A, Pel B or Pel C activities. Immunotitration revealed that Pel E accounted for a major fraction of the total extracellular Pel activity ranging from 40–60% in culture and potato tuber tissue. Isoelectric focusing of the extracellular Pels produced by various Echr strains indicated that while the Pel profiles of strains isolated from various hosts were different, the profiles of strains isolated from the same host were very similar. A significant proportion (ranging from 39 to 74%) of the Pel activity of these strains was inhibited by the anti-Pel E antibodies. DNA hybridization under stringent conditions indicated the presence of pelE homologous sequences in the genomes of E. chrysanthemi strains. We conclude that a Pel E-like enzyme occurs in all E. chrysanthemi strains examined.
Published Version
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