The largest database of trusted experimental protocols

α glucosidase ec3.2.1.20

Manufactured by Merck Group
Sourced in United States

α-glucosidase (EC3.2.1.20) is an enzyme that catalyzes the hydrolysis of terminal, non-reducing 1,4-linked α-D-glucose residues in polysaccharides, oligosaccharides, and α-glucosides. It is involved in the breakdown of complex carbohydrates and the release of glucose.

Automatically generated - may contain errors

4 protocols using α glucosidase ec3.2.1.20

1

α-Glucosidase Inhibition Assay with D. cycadina

Check if the same lab product or an alternative is used in the 5 most similar protocols
α-glucosidase (EC3.2.1.20) was obtained from Sigma Aldrich, and acarbose was obtained from Bayer, Pakistan. An ELISA Micro Plate Reader (Emax) from Molecular Devices and isolated compounds 15 from D. cycadina were used.
+ Open protocol
+ Expand
2

Enzymatic Characterization of α-Glucosidase

Check if the same lab product or an alternative is used in the 5 most similar protocols
All starting materials and reagents were purchased from commercial suppliers. α-glucosidase (EC 3.2.1.20) was purchased from Sigma-Aldrich. TLC was performed on Silica gel F-254. Melting points were measured on a microscopic melting point apparatus. The 1H NMR and 13 C NMR were measured (DMSO solution) with Bruker spectrometer (500 MHz 1H, 125 MHz 13 C). HRMS was performed on AB SCIEX Triple TOF 5600+ with electron spray ionisation (ESI) as the ion source.
+ Open protocol
+ Expand
3

Chemical Characterization and Biological Evaluation

Check if the same lab product or an alternative is used in the 5 most similar protocols
1H and 13 C NMR spectra were recorded on a Bruker AM500
spectrometer (Bruker, Karlsruhe, Germany). Melting points were measured on a Thomas
Scientific Capillary Melting Point Apparatus. MS and HR-MS were obtained on a JEOL JMS-700
mass spectrometer (JEOL, Tokyo, Japan). IR spectra were recorded on Varian 640-IR (Varian,
Inc., USA). Optical rotation was measured on a Perkin-Elmer 343 polarimeter (Perkin-Elmer,
Bridgeport, USA). Recycled HPLC and MPLC were conducted on Forte/R 100 (YMC Co., Ltd.,
Kyoto, Japan) using Triart C18 (S-5 µm, 12 nm and S-10 µm, 12 nm, YMC, Japan). Analytical
grade methanol, acetonitrile, and acetic acid for HPLC were purchased from Fisher (Fisher
Scientific Korea Ltd.). UV spectra and enzymatic assays were carried out on a SpectraMax
M3 Multi-Mode Microplate Reader (Molecular device, USA). α-Glucosidase (EC3.2.1.20) was
purchased from Sigma Aldrich St. Louis, USA. All chemicals were of analytical grade.
+ Open protocol
+ Expand
4

Antioxidant and Enzymatic Properties of Desi Onions

Check if the same lab product or an alternative is used in the 5 most similar protocols
Good quality and undamaged onions (Var. Desi Red, Phulkara) were obtained from a local market in Lahore, Pakistan. 1,1-diphenyl-2-picrylhydrazyl (DPPH), Na2CO3, MeOH, AlCl3, Folin-Ciocalteu's phenol reagent, potassium ferricyanide, potassium persulfate (K2S2O8), trichloroacetic acid, 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), ferrozine ferric chloride, FeCl2, hydrogen peroxide (H 2 O 2 ), Peroxidase from horseradish. Α-glucosidase (EC3-2.1.20) and α-amylase (EC-3.2.1.1) were bought from Sigma-Aldrich (St. Louis, MO, USA).
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!