The IPB has once again been recognized for its exemplary actions in terms of equal opportunity-oriented personnel and organizational policies and has received the TOTAL E-QUALITY certification for the…
The Plant Science Student Conference (PSSC) has been organised by students from the two Leibniz institutes, IPK and IPB, every year for the last 20 years. In this interview, Christina Wäsch (IPK) and…
Van Damme, E. J. M.; Hu, J.; Barre, A.; Hause, B.; Baggerman, G.; Rougé, P.; Peumans, W. J.;Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β-amylase from Calystegia sepium (hedge bindweed) rhizomesEur. J. Biochem.2686263-6273(2001)DOI: 10.1046/j.0014-2956.2001.02584.x
An abundant catalytically active β‐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 β‐amylases with regard to its amino‐acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β‐amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β‐amylase is a cytoplasmic vegetative storage protein.