Publication
Title
Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic -amylase from **Calystegia sepium** (hedge bindweed) rhizomes
Author
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.
Language
English
Source (journal)
European journal of biochemistry. - Berlin
Publication
Berlin : 2001
ISSN
0014-2956
Volume/pages
268:23(2001), p. 6263-6273
ISI
000172540800031
Full text (Publishers DOI)
Full text (publishers version - intranet only)
UAntwerpen
Faculty/Department
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 25.03.2015
Last edited 07.04.2017