An Accounting of Horseradish Peroxidase Isozymes Associated with the Cell Wall and Evidence that Peroxidase Does Not Contain Hydroxyproline
Open Access
- 1 December 1974
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 54 (6) , 870-876
- https://doi.org/10.1104/pp.54.6.870
Abstract
Isopycnic equilibrium centrifugation techniques were used to determine whether any horseradish (Amoracia lapathifolia) peroxidase isozymes were associated with hydroxyproline containing moieties. Purified peroxidase, horseradish root extracts, and peroxidase isozymes released from horseradish root cell walls were tested. In no case could any peak of peroxidase activity be found to band with hydroxyproline.Keywords
This publication has 9 references indexed in Scilit:
- Lignification in Trees: Indication of Exclusive Peroxidase ParticipationScience, 1973
- A preparative column electrophoresis apparatus using Sephadex G-25Analytical Biochemistry, 1971
- Role of Peroxidase when Hydroxyproline-rich Protein in Plant Cell Walls is increased by EthyleneNature New Biology, 1971
- Combined gradient-gel electrophoresis procedures for determining buoyant densities or sedimentation coefficients of all multiple forms of an enzyme simultaneouslyAnalytical Biochemistry, 1971
- Homovanillic acid as a fluorometric substrate for oxidative enzymes. Analytical applications of the peroxidase, glucose oxidase, and xanthine oxidase systemsAnalytical Chemistry, 1968
- A test for de novo synthesis of enzymes: density labeling with H2O18 of barley alpha-amylase induced by gibberellic acid.Proceedings of the National Academy of Sciences, 1967
- Oxidoreductive and hydrolytic enzyme patterns in plant suspension culture cellsExperimental Cell Research, 1967
- Peroxidase Isozymes from Horseradish RootsJournal of Biological Chemistry, 1966
- Oxygen Fixation into Hydroxyproline of Plant Cell Wall ProteinJournal of Biological Chemistry, 1963