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Antiglucosidase

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https://www.readbyqxmd.com/read/27867265/alpha-glucosidase-inhibitory-and-antioxidant-potential-of-antidiabetic-herb-alternanthera-sessilis-comparative-analyses-of-leaf-and-callus-solvent-fractions
#1
Tsun-Thai Chai, Chee-Siong Khoo, Chong-Siang Tee, Fai-Chu Wong
BACKGROUND: Alternanthera sessilis is a medicinal herb which is consumed as vegetable and used as traditional remedies of various ailments in Asia and Africa. OBJECTIVE: This study aimed to investigate the antiglucosidase and antioxidant activity of solvent fractions of A. sessilis leaf and callus. MATERIALS AND METHODS: Leaf and callus methanol extracts were fractionated to produce hexane, chloroform, ethyl acetate, butanol, and water fractions...
October 2016: Pharmacognosy Magazine
https://www.readbyqxmd.com/read/26642692/cytotoxicity-and-antiglucosidase-potential-of-six-selected-edible-and-medicinal-ferns
#2
Tsun-thai Chai, Loo-yew Yeoh, Nor Ismaliza Mohd Ismail, Hean-chooi Ong, Fai-chu Wong
No abstract text is available yet for this article.
March 2015: Acta Poloniae Pharmaceutica
https://www.readbyqxmd.com/read/25976787/water-fraction-of-edible-medicinal-fern-stenochlaena-palustris-is-a-potent-%C3%AE-glucosidase-inhibitor-with-concurrent-antioxidant-activity
#3
Tsun-Thai Chai, Meng-Tee Kwek, Hean-Chooi Ong, Fai-Chu Wong
This study aimed to isolate a potent antiglucosidase and antioxidant fraction from Stenochlaena palustris. Extraction was performed with hexane, chloroform, ethyl acetate, methanol, and water. Antiglucosidase, 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging and ferric reducing antioxidant power (FRAP) assays found methanol extract (ME) to be the most active. Water fraction (WF) of ME was a stronger α-glucosidase inhibitor (EC50 2.9 μg/mL) than quercetin, with weak antiamylase activity. WF was a competitive α-glucosidase inhibitor...
November 1, 2015: Food Chemistry
https://www.readbyqxmd.com/read/3546312/glucosidase-ii-a-protein-of-the-endoplasmic-reticulum-with-high-mannose-oligosaccharide-chains-and-a-rapid-turnover
#4
G J Strous, P Van Kerkhof, R Brok, J Roth, D Brada
Glucosidase II is regarded as a resident protein of the endoplasmatic reticulum. The enzyme removes alpha-1-3-linked glucose from high mannose oligosaccharides N-linked to asparagine residues of glycoproteins. Monospecific antibodies raised against the pig kidney enzyme are used to study the metabolism of the enzyme in a rat hepatoma cell line. These antiglucosidase II antibodies specifically immune precipitate glucosidase II as a 100,000-Da species from [35S]methionine-labeled cells. In addition, protein blotting and immune staining of cell extracts from both rat liver and human and rat hepatoma cell lines show identity in apparent Mr (100,000)...
March 15, 1987: Journal of Biological Chemistry
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