Maltitol and maltobionate act differently on maltose- and maltooligosaccharide hydrolysis by human small intestinal glucoamylase-maltase indicating two different enzyme binding modes

Archives of Biochemistry and Biophysics

Volumn 327, Issue 2, 1996, Pages 295-302

  Günther, Stephan ^a,b   Wehrspaun, Annelie ^a   Heymann, Herbert ^a  

^a HANNOVER MEDICAL SCHOOL   (Germany)

^b UNIVERSITY OF VETERINARY MEDICINE HANNOVER   (Germany)

Author keywords

Glucoamylase maltase; Maltitol; Maltobionate; Maltooligosaccharides; Small intestine

Indexed keywords

ALPHA GLUCOSIDASE; GLUCAN 1,4 ALPHA GLUCOSIDASE; INTESTINE ENZYME; MALTITOL; MALTOSE; OLIGOSACCHARIDE;

ARTICLE; CARBOHYDRATE METABOLISM; COMPETITIVE INHIBITION; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME SUBSTRATE; HUMAN; HYDROLYSIS; PRIORITY JOURNAL;

ALPHA-GLUCOSIDASES; BINDING SITES; BINDING, COMPETITIVE; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; DISACCHARIDES; HUMANS; HYDROLYSIS; INTESTINE, SMALL; KINETICS; MALTOSE; MATHEMATICS; MODELS, STRUCTURAL; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; SUGAR ALCOHOLS; TRISACCHARIDES;

EID: 0029968075     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.1996.0125     Document Type: Article

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