Maltase-glucoamylase

Glucoamylase complex (EC 3.2.1.20) Glucoamylase-(maltase)-l and glucoamylase-(maltase)-2 (have hiiisimilaf... 

Porcine-serum a-D-glucosidase exhibits glucoamylase activity. A simple procedure for isolating the glucoamylase-maltase complex from rabbit intestines by affinity chromatography on Sephadex G-200 has been reported. Other Sephadex gels did not bind the enzyme to any significant extent. 

L. Sim, K. Jayakanthan, S. Mohan, R. Nasi, B. D. Johnston, B. M. Pinto, and D. R. Rose, New glucosidase inhibitors from ayurvedic herbal treatment for type 2 diabetes Structures and inhibition of human intestinal maltase-glucoamylase with compounds from Salacia reticulata, Biochemistry, 49... 

Reaction of benzyl a-D-glucopyranosyl cyclic sulfate 44 or benzyl a-D-galactopyranosyl cyclic sulfate 45 with 1,4-anhydro-2,3,5-tri-0-benzyl-4-thio-D-arabinol 46, followed by debenzylation and reduction, gave novel sulfonium sulfate derivatives 47a and 47b, respectively, which were used to prepare homologs of salacinol 48, a natural human maltase glucoamylase inhibitor, as lead candidates for the treatment of type 2 diabetes (Scheme 3) <2006JOC1111>. 

Digestion of dietary glycogen and starch in the human body begins with the salivary and pancreatic amylases, which cleave a-1,4 linkages at random. It continues with a glucoamylase found in the brush border membranes of the small intestine where it occurs as a complex with maltase.74 Carbohydrases are discussed in Chapter 12, Section B. 

Exo-l,4-a-D-glucosidase, also called glucoamylase or maltase, catalyzes sequential hydrolysis of terminal glucosyl units linked in a(l 4) linkages from the nonreducing ends of malto-oligosaccharides or maltose. 

Maltase. Glucoinvertase. Glucosidosucrase. Maltase-glucoamylase. Hydrolysis of terminal, non-reducing 1,4-linked D-glucose residues... 

Individuals with genetic deficiencies of the sucrase-isomaltase complex show symptoms of sucrose intolerance but are able to digest normal amounts of starch in a meal, without problems. The maltase activity in the glucoamylase complex, and residual activity in the sucrase-isomaltase complex (which is normally present in excess of need) is apparently sufficient to digest normal amounts of dietary starch. 

The isoenzymes of a-D-glucosidases have been studied in human white blood cells by immunological and electrophoretic techniques.Three isoenzymes have been found in leucocyte extracts lysosomal a-D-glucosidase ( acid maltase, glucoamylase), cytoplasmic neutral oi-D-glucosidase, and an enzyme immuno-logically identical to renal maltase (a-D-glucosidase). In Pompe s disease and other types of acid maltase deficiency, the deficiency is as complete in leucocytes as in other tissues, and the residual activity is due to renal maltase . 

C13H25NO10 355.341 Alkaloid from Corrmwlina communis, Aglaonema treubii, Hyadnthus orientalis and Lobelia sessilifolia. Potent a-glucosidase inhibitor, competitive inhibitor for intestinal sucrase. Also inhibits maltase, trehalase, glucoamylase and a-amylase. Antidiabetic agent. Amorph. powder -t IH2O. 

An acid a-D-glucosidase in human liver has been purified by adsorption onto Sephadex, followed by desorption with methyl a-D-glucopyranoside, a competitive inhibitor.The enzyme (p/4.58) was shown to be homogeneous by ultracentrifugation and disc gel electrophoresis. Guanidinium hydrochloride, but not urea, dissociated the enzyme. The glucoamylase activity, but not the maltase activity, was inhibited by methyl a-D-glucopyranoside. 

The isolation of a maltase-glucoamylase complex from rabbit intestines has been described. ... 

An acid a-D-glucosidase activity isolated from human liver exhibits glucoamylase activity, which was competitively inhibited by methyl a-D-glucopyranoside, and maltase activity. ... 

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