Action of salivary α-amylase on amylopectin and glycogen

William J. Whelan, P. J P Roberts

Research output: Contribution to journalArticle

8 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)748-749
Number of pages2
JournalNature
Volume170
Issue number4331
DOIs
StatePublished - Dec 1 1952
Externally publishedYes

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Amylopectin
Amylases
Glycogen
Amylose
Maltose
Enzymes
maltotriose

ASJC Scopus subject areas

  • General

Cite this

Action of salivary α-amylase on amylopectin and glycogen. / Whelan, William J.; Roberts, P. J P.

In: Nature, Vol. 170, No. 4331, 01.12.1952, p. 748-749.

Research output: Contribution to journalArticle

Whelan, William J. ; Roberts, P. J P. / Action of salivary α-amylase on amylopectin and glycogen. In: Nature. 1952 ; Vol. 170, No. 4331. pp. 748-749.
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