Title
Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic <tex>$\beta$</tex>-amylase from **Calystegia sepium** (hedge bindweed) rhizomes Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic <tex>$\beta$</tex>-amylase from **Calystegia sepium** (hedge bindweed) rhizomes
Author
Faculty/Department
Faculty of Sciences. Biology
Publication type
article
Publication
Berlin ,
Subject
Chemistry
Biology
Source (journal)
European journal of biochemistry. - Berlin
Volume/pages
268(2001) :23 , p. 6263-6273
ISSN
0014-2956
ISI
000172540800031
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
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.
E-info
https://repository.uantwerpen.be/docman/iruaauth/c1d8d3/0089677.pdf
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