Results 331 to 340 of about 83,616 (370)
Some of the next articles are maybe not open access.

ALPHA-GLUCOSIDASE INHIBITORS

Endocrinology and Metabolism Clinics of North America, 1997
Alpha-glucosidase inhibitors are antihyperglycemic agents that lower blood glucose by delaying the digestion and absorption of complex carbohydrates. They are competitive inhibitors of the enzymes in the brush border of enterocytes that cleave eligosaccharides to monosaccharides.
openaire   +2 more sources

α-Glucosidase I

1994
Abstract Initial studies on partially purified a-glucosidase I from rat liver1·2 and oviduct microsomes3  .4 demonstrated that this enzyme removes a single glucose residue from Glc3Man9GlcNAc2. a-Glucosidase I was subsequently purified from calf5 and porcine6 liver, lactating bovine mammary tissue7, mung bean seedlings8, and 5 ...
R Trimble, K Moremcn,, A Herscovics
openaire   +1 more source

On the Glucosidases of the Intestine of the Pig.

Acta Physiologica Scandinavica, 1943
Summary.An investigation is made of the glucosidases of the small intestine and the duodenum of the pig. It is shown that both α‐and β‐glucosidase occur, and the pH‐activity curves of both enzymes are determined.
Gunnar Steensholt, Stig. Veibel
openaire   +2 more sources

Reversible inhibitors of .beta.-glucosidase

Biochemistry, 1985
A variety of reversible inhibitors of sweet almond beta-glucosidase were examined. These included simple sugars and sugar derivatives, amines and phenols. With respect to the sugar inhibitors and, indeed, the various glycoside substrates, the enzyme has what can be considered a "relaxed specificity".
Harry E. Ensley   +4 more
openaire   +3 more sources

Design and Synthesis of Labystegines, Hybrid Iminosugars from LAB and Calystegine, as Inhibitors of Intestinal α-Glucosidases: Binding Conformation and Interaction for ntSI.

Journal of Organic Chemistry, 2015
This paper identifies the required configuration and orientation of α-glucosidase inhibitors, miglitol, α-1-C-butyl-DNJ, and α-1-C-butyl-LAB for binding to ntSI (isomaltase).
A. Kato   +13 more
semanticscholar   +1 more source

Studies on the glucosidase “linamarase”

Phytochemistry, 1965
Abstract From infra-red spectra it was confirmed that the cyanogenic glucosides linamarin and lotaustralin are β-linked. A survey of the β-glucosidase activity of enzyme extracts from a variety of higher plants revealed that the ability to hydrolyse linamarin and lotaustralin was very limited.
G.W. Butler, L.D. Kennedy, R.W. Bailey
openaire   +2 more sources

Acarbose: An α-glucosidase inhibitor

American Journal of Health-System Pharmacy, 1996
The chemistry, pharmacology, pharmacokinetics, and clinical efficacy of acarbose, a new antidiabetic agent, are reviewed. Acarbose reversibly inhibits intestinal alpha-glucosidases, enzymes responsible for the metabolism of complex carbohydrates into absorbable monosaccharide units.
Anne E. Martin, Patricia A. Montgomery
openaire   +2 more sources

Unconventional β-Glucosidases: A Promising Biocatalyst for Industrial Biotechnology

Applied Biochemistry and Biotechnology, 2021
Ravish Godse   +3 more
semanticscholar   +1 more source

A Spectrophotometric Assay for Glucosidase I

Analytical Biochemistry, 1994
A spectrophotometric assay for glucosidase I using the synthetic trisaccharide alpha-D-Glc 1-->2 alpha-D-Glc 1-->3 alpha-D-Glc-O(CH2)8COOCH3 is reported. The terminal glucose is released from the substrate by the enzyme and quantitated using glucose oxidase, peroxidase, and o-dianisidine. The trisaccharide is specific for glucosidase I and provides all
Christine H. Scaman   +5 more
openaire   +3 more sources

Alpha-glucosidases in human urine

Clinica Chimica Acta, 1967
Abstract Two α-glucosidases from human urine have been separated by means of Sephadex G-200 gel filtration and further purified by DEAE-Sephadex chromatography. Both enzymes hydrolyse maltose and glycogen to free glucose. Indirect evidence has been obtained of the possible occurrence of further α-glucosidases in human urine.
C. Franzini, P.A. Bonini
openaire   +3 more sources

Home - About - Disclaimer - Privacy