Plasma membrane bound high pI peroxidase isoenzymes convert tryptophan to indole-3-acetaldoxime
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Contributors
Abstract
-Several peroxidase isoenzymes (pI 8-9) from phase-partitioned Chinese cabbage plasma membrane oxidized l-tryptophan to indole-3-acetaldoxime as shown by (i) correlation of catalytic activity with benzidineguaiacol staining on isoelectric focussing (IEF) gels, (ii) inhibition of enzyme activity by polyclonal antisera directed against tobacco peroxidase isoenzymes (which cross-react with Chinese cabbage peroxidases) and (iii) inhibition of tetraguaiacol formation by l-tryptophan. Treatment of the outside-out plasma membrane vesicles with 1 M sodium chloride and sonification released only part of the membrane-bound tryptophan oxidizing enzyme activity, suggesting little non-specific binding of peroxidases to (or trapping in) the membrane vesicles.
Details
Original language | English |
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Pages (from-to) | 1397-1400 |
Number of pages | 4 |
Journal | Phytochemistry |
Volume | 29 |
Issue number | 5 |
Publication status | Published - 1990 |
Peer-reviewed | Yes |
Externally published | Yes |
Keywords
ASJC Scopus subject areas
Keywords
- Brassica campestris subsp. pekinensis, Brassicaceae, Chinese cabbage, indole-3-acetaldoxime peroxidase isoenzymes, l-tryptophan.