Related Experiment Video
Updated: Aug 10, 2026
Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 31, 2013
Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic beta-amylase
1Laboratory 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.
