Starch Phosphorylase Inhibitor Is beta-Amylase |
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Authors: | Pan S M Chang T C Juang R H Su J C |
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Institution: | Department of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan 10764, ROC. |
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Abstract: | The proteinaceous noncompetitive inhibitor of starch phosphorylase isolated from the root of sweet potato (Ipomoea batatas L.] Lam.) (TC Chang, JC Su 1986 Plant Physiol 80: 534-538) has been identified as a β-amylase. The starch phosphorylase inhibitor and β-amylase activities copurified to give a protein indistinguishable from commercial β-amylase by electrophoretic and immunological methods, and the two activities showed parallel responses in pH, temperature, and inhibitor sensitivity tests. The amylolytic pattern of the inhibitor corresponded to that of β-amylase and its inhibitory effect toward starch phosphorylase was due to neither deprivation of starch, the primer for the phosphorylase assay, nor the inhibitory effect of amylolytic products. |
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