Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β-amylase from Calystegia sepium (hedge bindweed) rhizomes.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
  • Additional Information
    • Subject Terms:
    • Abstract:
      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. [ABSTRACT FROM AUTHOR]
    • Abstract:
      Copyright of European Journal of Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)