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

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    • Abstract:
      An abundant catalytically active β-amylase (EC 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:
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