Inhibitors of polygalacturonase in calli of Orobanche aegyptiaca

• Published in: Phytochemistry (Oxford) Vol. 45; no. 6; pp. 1115 - 1121
• Main Authors: Ben-Hod, Graham, Nun, Nurit Bar, Tzaban, Salit, Mayer, A.M.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Ltd 01-07-1997; Elsevier
• Subjects: Biological and medical sciences; Biotechnology; calli; Cells, Cultured; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors - isolation & purification; Enzyme Inhibitors - pharmacology; Fundamental and applied biological sciences. Psychology; inhibitors; Orobanchaceae; Orobanche aegyptiaca; Parasitic plants; Parasitic plants. Weeds; Parasitism; Parasitism and symbiosis; Phytopathology. Animal pests. Plant and forest protection; Plant physiology and development; Plant Roots; Plants - enzymology; Plants - parasitology; polygalacturonase; Polygalacturonase - antagonists & inhibitors; Orobanchaceae; Orobanche aegyptiaca; inhibitors; calli; polygalacturonase; Callus; Purification; Enzyme; Enzyme inhibitor; Polygalacturonase; Characterization; Enzymatic activity; Dicotyledones; Glycosidases; Angiospermae; Hydrolases; Spermatophyta; O-Glycosidases; Parasitic plant
• ISSN: 0031-9422; 1873-3700
• DOI: 10.1016/S0031-9422(97)00134-9

The presence of at least three distinct polygalacturonases (PGase) in callus of
Orobanche was demonstrated. The PGase activity is labile and at pH 4.5 does not require activation by cations. It can be partially purified on Biogel P 100 columns and can be resolved by PAGE into several bands. Broomrape callus tissue also contains inhibitors of PGase activity. One of these is a low
M
r
compound, stable to boiling and removable by dialysis. An additional inhibitor precipitable by ammonium sulphate is also present. © 1997 Elsevier Science Ltd. All rights reserved