Affordable Access

Publisher Website

Partial Purification and Properties of Soluble Ascorbate Peroxidases From Pea Leaves

Authors
Journal
Journal of Plant Physiology
0176-1617
Publisher
Elsevier
Publication Date
Volume
115
Issue
1
Identifiers
DOI: 10.1016/s0176-1617(84)80051-6
Keywords
  • Pisum Sativum
  • Hydrogen Peroxide
  • Ascorbate Peroxidases
Disciplines
  • Biology
  • Design

Abstract

Summary One nonenzymic and two enzymic forms of ascorbate peroxidase were found in pea leaves, and designated A, B and C. Form A was due to a low molecular weight, heat-stable component, and could be separated from the enzymic forms by gel filtration. Forms B and C were soluble proteins with an apparent molecular weight of 57,000. These two forms could be separated by cation-exchange chromatography on CM-Sephadex C-50. This technique was incorporated into a procedure for their partial purification. Several properties of B and C were found to be similar: they were active over a wide pH range (5 to 8), they displayed very high affinities for H 2O 2 (Km<5 μM), and Km values for ascorbate (6.5 mM and 2.9 mM, respectively) were comparable to physiological concentrations of this substrate. These properties are considered conducive to the proposed physiological role of ascorbate peroxidase, viz prevention of H 2O 2 accumulation.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Partial purification and properties of soluble asc...

on Journal of Plant Physiology June 1984

[Partial purification and properties of soluble "b...

on Biokhimii︠a︡ (Moscow, Russia) 1972

Purification and properties of a 4-methylene-L-glu...

on Journal of Biological Chemistr... Jul 25, 1983

Purification and properties of NADP-dependent mala...

on Biochimica et Biophysica Acta... Jan 01, 1983
More articles like this..