JXB Advance Access originally published online on July 2, 2004
Journal of Experimental Botany 2004 55(403):1655-1662; doi:10.1093/jxb/erh197
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
RESEARCH PAPER |
Biochemical and immunochemical evidences for the presence of lipoxygenase in plant mitochondria
1Section of Plant Biology, Department of Biology and Agro-industrial Economics, University of Udine, via Cotonificio 108, I-33100 Udine, Italy
2Department of Chemical Science and Technology, University of Udine, via Cotonificio 108, I-33100 Udine, Italy
* To whom correspondence should be addressed. Fax: +39 0432 558784. E-mail: biolveg{at}dbea.uniud.it
In this paper, both biochemical and immunochemical evidence for the presence of lipoxygenase (LOX) in plant mitochondria is presented. Highly purified pea (Pisum sativum L., cv. Alaska) mitochondria show LOX activity, evaluated as conjugated diene formation, oxygen consumption, and hydroperoxide formation. Both 9- and 13-hydroperoxy-octadecadienoic acids are produced by the oxidation of linoleic acid. LOX activity is particularly evident in swollen mitochondria; it is inhibited by nordihydroguaiaretic acid, a pea anti-LOX B antibody, and has two pH optima (6.0 and 7.5). A mitochondrial protein of
97 kDa cross-reacts with a pea seed anti-LOX B antibody. This reaction is detectable in both soluble (matrix fraction) and membrane-bound (submitochondrial particles) proteins. Considering that pea mitochondria were extracted from actively growing stems that were differentiating tube elements, it is suggested that the presence of LOX in these organelles may be related to their degradation linked to xylem differentiation.
Key words: Lipoxygenase, mitochondria, Pisum sativum L.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
G. Mita, A. Quarta, P. Fasano, A. De Paolis, G. P. Di Sansebastiano, C. Perrotta, R. Iannacone, E. Belfield, R. Hughes, N. Tsesmetzis, et al. Molecular cloning and characterization of an almond 9-hydroperoxide lyase, a new CYP74 targeted to lipid bodies J. Exp. Bot., September 1, 2005; 56(419): 2321 - 2333. [Abstract] [Full Text] [PDF] |
||||
