Literature DB >> 302742

The action pattern of human salivary alpha-amylase in the vicinity of the branch points of amylopectin.

M Abdullah, W J Whelan, B J Catley.   

Abstract

Salivary alpha-amylase hydrolyses amylopectin in stages. At the end of the so-called second stage, there are present glucose, maltose, and a series of alpha-limit dextrins containing (1 leads to 4)- and (1 leads to 6)-alpha-D-glucosidic bonds. The structures of the limit dextrins containing a single (1 leads to 6)-bond were examined. Six such dextrins were found. Of these, two were capable of being further hydrolysed by alpha-amylase, whereas the remaining four were true, amylase-resistant alpha-limit dextrins. The structures of the limit dextrins afforded information about those (1 leads to 4)-alpha-D-glucosidic bonds of amylopectin that are capable of being cleaved by salivary alpha-amylase and those that are resistant. In order to define further the action of alpha-amylase, the alpha-amylolytic products of 6-alpha-maltotriosyl-D-glucose, 6(3)-alpha-maltotriosylmaltotriose, and 6(3)-alpha-maltotriosylmaltotetraose were examined.

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Year:  1977        PMID: 302742     DOI: 10.1016/s0008-6215(00)81937-0

Source DB:  PubMed          Journal:  Carbohydr Res        ISSN: 0008-6215            Impact factor:   2.104


  2 in total

1.  Alpha-amylase structure and activity.

Authors:  E A MacGregor
Journal:  J Protein Chem       Date:  1988-08

2.  Modulation of starch digestion for slow glucose release through "toggling" of activities of mucosal α-glucosidases.

Authors:  Byung-Hoo Lee; Razieh Eskandari; Kyra Jones; Kongara Ravinder Reddy; Roberto Quezada-Calvillo; Buford L Nichols; David R Rose; Bruce R Hamaker; B Mario Pinto
Journal:  J Biol Chem       Date:  2012-07-31       Impact factor: 5.157

  2 in total

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