Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1979 Apr;63(4):696–699. doi: 10.1104/pp.63.4.696

Indole-3-acetic Acid Oxidase from Peas

I. Occurrence and Distribution of Peroxidative and Nonperoxidative Forms 1

Stephen D Bryant a,2, Forrest E Lane a
PMCID: PMC542899  PMID: 16660794

Abstract

Tissues of etiolated pea seedlings variety Alaska were examined for the presence of peroxidative and nonperoxidative forms of indoleacetic acid (IAA) oxidase. Enzymes were extracted in a sequence involving acetone powder preparation from pea tissues, buffer extraction of the powder, ammonium sulfate precipitation, dialysis, lyophilization, and acrylamide gel electrophoresis. Electrophoretically separable proteins were assayed for IAA oxidase activity with the Salkowski test, and peroxidase activity was based on the color reaction with benzidine and H2O2. Each tissue examined contained several nonperoxidative IAA oxidases. No tissue contained more than three peroxidative IAA oxidases, whereas the plumule hooks (a tissue with a high IAA oxidase activity) contained no detectable peroxidases. The results indicate that nonperoxidative IAA oxidases might play a major role in the regulation of IAA content in pea seedlings.

Full text

PDF
696

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  2. DIXON M. A nomogram for ammonium sulphate solutions. Biochem J. 1953 Jun;54(3):457–458. doi: 10.1042/bj0540457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hoyle M. C. High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing. Plant Physiol. 1977 Nov;60(5):787–793. doi: 10.1104/pp.60.5.787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hoyle M. C. Indoleacetic Acid oxidase: a dual catalytic enzyme? Plant Physiol. 1972 Jul;50(1):15–18. doi: 10.1104/pp.50.1.15. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kerstetter R. E., Keitt G. W. Direct Assay of IAA Decarboxylation Rate in Excised Tobacco Pith: Relation to Aging. Plant Physiol. 1966 May;41(5):903–904. doi: 10.1104/pp.41.5.903. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Macnicol P. K. Peroxidases of the Alaska pea (Pisum sativum L.). Enzymic properties and distribution within the plant. Arch Biochem Biophys. 1966 Nov;117(2):347–356. doi: 10.1016/0003-9861(66)90422-x. [DOI] [PubMed] [Google Scholar]
  8. Manning D. T., Galston A. W. On the Nature of the Enzymatically Catalyzed Oxidation Products of Indoleacetic Acid. Plant Physiol. 1955 May;30(3):225–231. doi: 10.1104/pp.30.3.225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Sequeira L., Mineo L. Partial purification and kinetics of indoleacetic Acid oxidase from tobacco roots. Plant Physiol. 1966 Sep;41(7):1200–1208. doi: 10.1104/pp.41.7.1200. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Siegel B. Z., Galston A. W. Indoleacetic acid oxidase activity of apoperoxidase. Science. 1967 Sep 29;157(3796):1557–1559. doi: 10.1126/science.157.3796.1557. [DOI] [PubMed] [Google Scholar]
  11. Siegel B. Z., Galston A. W. The isoperoxidases of Pisum sativum. Plant Physiol. 1967 Feb;42(2):221–226. doi: 10.1104/pp.42.2.221. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES