Abstract
Utilizing starch-gel electrophoresis, 12 discrete peroxidases were identified in purified extracts of the dwarf tomato shoot (Lycopersicon esculentum). Nine of the peroxidases moved toward the anode while 3 moved toward the cathode. In addition, a continuous peroxidase smear was separated from the above 12 peroxidases. This smear moved toward the anode and accounted for 50% of the total peroxidase activity in the crude extract.
Four of the major peroxidases were isolated and partially purified, using acetone and ammonium sulfate precipitations, preparative starch-gel electrophoresis and chromatography on DEAE and CM-cellulose.
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- 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]
- 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]
- SMITHIES O. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem J. 1955 Dec;61(4):629–641. doi: 10.1042/bj0610629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shannon L. M., Kay E., Lew J. Y. Peroxidase isozymes from horseradish roots. I. Isolation and physical properties. J Biol Chem. 1966 May 10;241(9):2166–2172. [PubMed] [Google Scholar]
- 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]