Egg plant lipoxygenase: Isolation and partial characterization

S. Grossman, M. Trop, R. Avtalion, A. Pinsky

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Egg plant lipoxygenase EC 1.13.1.13 when purified on Ecteola cellulose was resolved into two active fractions with most of the activity in the first fraction (A). This fraction when further purified on Sephadex G200-120 had 20 times the specific activity of the crude material. It proved to be a single substance by electrophoresis and immunological technique. The pH optimum was 6.5. Its activity was specific for the cis,cis-1,4 pentadiene structure. There was no inhibition by cyanide, azide, EDTA or fluoride. Nordihydroguaretic acid, on the other hand, exhibited strong inhibition at 3 × 10-3M concentration. The specific antibody caused 50% inhibition.

Original languageEnglish
Pages (from-to)467-473
Number of pages7
JournalLipids
Volume7
Issue number7
DOIs
StatePublished - Jul 1972

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