Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic beta-amylase from Calystegia sepium (hedge bindweed) rhizomes. |
| |
| Authors: | E J Van Damme J Hu A Barre B Hause G Baggerman P Rougé W J Peumans |
| |
| Affiliation: | Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Leuven, Belgium. Els.VanDamme@agr.kuleuven.ac.be |
| |
| Abstract: | An abundant catalytically active beta-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant beta-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the beta-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome beta-amylase is a cytoplasmic vegetative storage protein. |
| |
| Keywords: | |
|
|
