INACTIVATION OF THE PEROXIDASE ISOENZYME GROUPS, APRX AND LPL BPRX, MARKERS OF THE IN-VITRO CULTURE OF GRAPEVINE, BY FOSETYL-AL (ALUMINUM TRIS[ETHYL PHOSPHONATE])

Citation
Ml. Serrano et al., INACTIVATION OF THE PEROXIDASE ISOENZYME GROUPS, APRX AND LPL BPRX, MARKERS OF THE IN-VITRO CULTURE OF GRAPEVINE, BY FOSETYL-AL (ALUMINUM TRIS[ETHYL PHOSPHONATE]), Journal of plant physiology, 149(1-2), 1996, pp. 149-152
Citations number
15
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
01761617
Volume
149
Issue
1-2
Year of publication
1996
Pages
149 - 152
Database
ISI
SICI code
0176-1617(1996)149:1-2<149:IOTPIG>2.0.ZU;2-J
Abstract
Grapevine (Vitis vinifera cv. Monastrell) fruits contain, as the only component of peroxidase polymorphism, the peroxidase isoenzyme B-5, wh ich is the sole component of the peroxidase isoenzyme group HpI BPrx i n grapevines. Establishment of suspension cell cultures from grapevine fruits is accompanied by the de novo expression of one acidic (APrx) and one basic (LpI BPrx) peroxidase isoenzyme group in the culture med ium, which indicates that the in vitro culture is associated with the new expression of two groups of cell wall-located peroxidase isoenzyme s. Treatment of suspension cultured cells with aluminum tris [ethyl ph osphonate] (fosetyl-Al) reduces the level of peroxidase activity found in the culture medium, this effect being specific to those isoenzymes that are expressed de novo during cell culture, the isoenzyme groups APrx and LpI BPrx. Thus, fosetyl-Al selectively inactivates the peroxi dase isoenzyme groups, APrx and LpI BPrx, which are markers of the pro cess that accompanies the establishment of grapevine cell cultures.