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- Title
Lupin peroxidases. II. Binding of acidic isoperoxidases to cell walls.
- Authors
Ros Barceló, Alfonso; Pedreño, M. Angeles; Muñoz, Romualdo; Sabater, Francisco
- Abstract
Extracellular acidic isoperoxidases (EC 1.11.1.7), isolated from both the cell walls and intercellular spaces of lupin (Lupinus albus L. cv. multolupa) hypocotyls, bound to water-insoluble pectins of wall fragments also isolated from the hypocotyls. The binding was saturable by increasing the isoenzyme concentration in the assay medium and it was dependent on the pH; neutral pH (6.0-7.0) favoured release, while acidic pH (4.0-5.0) favoured the attachment to the cell wall. Binding of acidic isoperoxidases to wall fractions was correlated with the in vitro acid-induced growth of hypocotyl segments, and both were modulated in the same direction by the Ca2+/H+ ratio in the incubation media, although the two responses were clearly separated when the Ca2+/H+ ratio varied. Binding of acidic isoperoxidases of cell walls could operate as a fine control of the activity of these cell wall enzymes, although its physiological role in the cell wall stiffening remains unclear. Some aspects of Ca2+ on the control of peroxidase activity at this level are also discussed.
- Subjects
PLANT cell walls; EFFECT of acids on plants; PLANT physiology; CALCIUM compounds; PLANT enzymes; PROTEIN binding
- Publication
Physiologia Plantarum, 1988, Vol 73, Issue 2, p238
- ISSN
0031-9317
- Publication type
Article
- DOI
10.1111/j.1399-3054.1988.tb00592.x