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])
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
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.