Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic beta-amylase from Calystegia sepium (hedge bindweed) rhizomes.
Eur J Biochem
; 268(23): 6263-73, 2001 Dec.
Article
en En
| MEDLINE
| ID: mdl-11733023
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Beta-Amilasa
/
Magnoliopsida
Idioma:
En
Revista:
Eur J Biochem
Año:
2001
Tipo del documento:
Article
País de afiliación:
Bélgica
Pais de publicación:
Reino Unido