Abstract
Roberts and Whelan1 have shown that the action of salivary α-amylase on amylose is consistent with the view that the enzyme can hydrolyse any except the terminal α-1 : 4-linkages. This leads to the formation of maltose and maltotriose. Similar studies using the linear maltodextrins2 have confirmed this hypothesis3. We now wish to make a preliminary report of the action of this enzyme on glycogen and amylopectin.
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References
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Peat, S., Whelan, W. J., Hobson, P. N., and Thomas, Gwen J., J. Chem. Soc. (in the press).
Peat, S., Whelan, W. J., and Thomas, Gwen J., J. Chem. Soc. (in the press).
Peat, S., Roberts, P. J. P., and Whelan, W. J., Biochem. J., 51, xvii (1952).
Peat, S., Roberts, P. J. P., and Whelan, W. J., J. Chem. Soc. (in the press).
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WHELAN, W., ROBERTS, P. Action of Salivary α-Amylase on Amylopectin and Glycogen. Nature 170, 748–749 (1952). https://doi.org/10.1038/170748a0
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DOI: https://doi.org/10.1038/170748a0
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