Plant Physiol. Drug Metab Dispos
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 49:716-721 (1972)
© 1972 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vickery, L. E.
Right arrow Articles by Purves, W. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vickery, L. E.
Right arrow Articles by Purves, W. K.
Agricola
Right arrow Articles by Vickery, L. E.
Right arrow Articles by Purves, W. K.
Articles

Isolation of Indole-3-ethanol Oxidase from Cucumber Seedlings 1

Larry E. Vickery2 and William K. Purves

a Department of Biological Sciences, University of California, Santa Barbara, California 93106

Previous work in this laboratory has shown that cucumber (Cucumis sativus L.) seedlings contain large amounts, relative to other indolic compounds, of extractable indole-3-ethanol (IEt); tracer studies have established that IEt is metabolized to IAA. We have now succeeded in isolating an enzyme from these seedlings which catalyzes the oxidation of IEt to indole-3-acetaldehyde (IAAld). The identification of the product as IAAld was based on solvent partitioning of the free aldehyde and its bisulfite adduct and radiochromatography following incubation of enzyme with 14C-IEt. A novel, quantitative colorimetric test for IAAld was also developed utilizing the Salkowski reagent. Partial purification of the enzyme was achieved by salt gradient chromatography on Bio-Rex 70, heating the preparation to 70 C, and chromatography on Sephadex G-150. This purification procedure yielded an enzyme activity purified in excess of 3000-fold, and studies on a standardized Sephadex column suggest a molecular weight of the enzyme of approximately 105,000. The reaction was found to proceed only aerobically; and, in the absence of other electron acceptors, O2 appears to be reduced to H2O2. The enzyme has nearly maximum activity from pH 8 to 11.

2 National Defense Education Act predoctoral fellow. Present address: USDA/ARS Western Regional Research Laboratory, Berkeley, Calif. 94710.

1 Supported by National Science Foundation Grant GB 13219.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1972 by the American Society of Plant Biologists