The inhibitory effect of the silver nanoparticles on yeast alpha glucosidase (Sigma, St. Louis, MO, USA) was determined using the method previously described in [37 (link)]. Briefly, 100 µL of the sample (AgNPs or acarbose) at different concentrations (from 10 to 120 µg/mL) was mixed separately with 50 µL of α glucosidase (0.1 U/mL), and incubated at 37 °C for 20 min. Then, 10 µL of p-nitrophenyl-α-d-glucopyranoside (pNPG) was added and incubated for 10 min under the same conditions. To stop the reaction, we added 650 µL of 1 M sodium carbonate Na2CO3. The absorbance was measured at 405 nm. The percentage of enzyme inhibition was calculated as I (%) = (A405Control − A405AgNPs/A405Control) × 100.
Yeast α glucosidase
Manufactured by Merck Group
Sourced in United States, Germany
Yeast α-glucosidase is an enzyme that catalyzes the hydrolysis of terminal, non-reducing α-D-glucose residues in α-D-glucosides. It is commonly used in laboratory settings for various biochemical and enzymatic analyses.
Automatically generated - may contain errors
Lab products found in correlation
Acarbose, by Merck Group (16 mentions)
P nitrophenyl α d glucopyranoside, by Merck Group (12 mentions)
Dithiothreitol (dtt), by Bio-Rad (7 mentions)
Quercetin, by Merck Group (5 mentions)
P nitrophenyl phosphate, by Merck Group (5 mentions)
Gallic acid, by Merck Group (4 mentions)
2 2 diphenyl 1 picrylhydrazyl (dpph), by Merck Group (4 mentions)
Penicillin streptomycin, by Thermo Fisher Scientific (4 mentions)
Ursolic acid, by Merck Group (4 mentions)
Porcine pancreatic amylase, by Merck Group (4 mentions)
Rosiglitazone, by Merck Group (3 mentions)
3 4 dihydroxy l phenylalanine dopa, by Merck Group (3 mentions)
P nitrophenyl α d glucopyranoside pnpg, by Merck Group (3 mentions)
Kojic acid, by Merck Group (3 mentions)
Mushroom tyrosinase, by Merck Group (3 mentions)
Ethylenediaminetetraacetic acid, by Merck Group (3 mentions)
Dimethyl sulfoxide (dmso), by Merck Group (3 mentions)
Non essential amino acids (neaa), by Thermo Fisher Scientific (3 mentions)
Human insulin, by Eli Lilly (3 mentions)
Trolox, by Merck Group (2 mentions)
39 protocols using yeast α glucosidase
1
Evaluating Silver Nanoparticle Inhibition of Yeast α-Glucosidase
2
Comprehensive Biochemicals for Metabolic Research
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Streptozotocin (≥98%), 2,2 diphenyl-1-1-picryl hydrazyl (DPPH), 4-nitro phenyl alpha-D- glucopyranoside, yeast alpha-glucosidase, acarbose, gallic acid, tannic acid, quercetin, trolox, diprotin A, suramin, beta-sitosterol, phloretin 2′glucoside, oleanolic acid, rosiglitazone, metformin, cytochalasin B, 2-deoxyglucose, 3-isobutyl-1-methylxanthine (IBMX), dexamethasone, insulin, dimethyl sulphoxide (DMSO) and all other chemicals and biochemicals unless otherwise noted were from Sigma (St. Louis, MO, USA). 2-deoxy-d-[3H]-glucose (2-DG) was from GE Healthcare, UK. All the positive controls used were of HPLC grade.
3
In Vitro Assay for SGSH-Fc Fusion Proteins
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Example 8
This example provides an alternative in vitro activity assay for SGSH-Fc fusion proteins. The assay is adapted from Karpova et al., J. Inherit. Metab. Dis., 19:278-285 (1996).
The standard reaction mixtures consisted of 10-15 μg of protein and 20 μL MU-α-GlcN5 (5 or 10 mmol/L, respectively) in Michaelis' barbital sodium acetate buffer, pH 6.5 (29 mmol/L sodium barbital, 29 mmol/L sodium acetate, 0.68% (w/v) NaCl, 0.02% (w/v) sodium azide; adjusted to pH 6.5 with HCl) and the reaction mixtures were incubated for 17 h at 37° C. MU-α-GlcNS is available from Moscerdam Substrates. After the first incubation, 6 μl twice-concentrated McIlvain's phosphate/citrate buffer, pH 6.7, containing 0.02% sodium azide and 10 μl (0.1 U) yeast a-glucosidase (Sigma) in water were added and a second incubation of 24 h at 37° C. was carried out. Long incubations at 37° C. (17-24 h) were carried out in 96-well plates which were sealed airtight with broad sticky tape, limiting evaporation to <15%. Next, 200 μL 0.5 mol/L Na2CO3/NaHCO3, pH 10.7, was added, and the fluorescence of the released 4-methylumbelliferone (MU) was measured on a Fluoroskan (Titertek) fluorimeter. Protein was determined as described previously (van Diggelen et al., Clin. Chim. Acta., 187:131-139 (1990)).
4
In Vitro SGSH-Fc Fusion Protein Activity Assay
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Example 8
This example provides an alternative in vitro activity assay for SGSH-Fc fusion proteins. The assay is adapted from Karpova et al., J. Inherit. Metab. Dis., 19:278-285 (1996).
The standard reaction mixtures consisted of 10-15 μg of protein and 20 μL MU-α-GlcNS (5 or 10 mmol/L, respectively) in Michaelis' barbital sodium acetate buffer, pH 6.5 (29 mmol/L sodium barbital, 29 mmol/L sodium acetate, 0.68% (w/v) NaCl, 0.02% (w/v) sodium azide; adjusted to pH 6.5 with HCl) and the reaction mixtures were incubated for 17 h at 37° C. MU-α-GcNS is available from Moscerdam Substrates. After the first incubation, 6 μl twice-concentrated McIlvain's phosphate/citrate buffer, pH 6.7, containing 0.02% sodium azide and 10 μl (0.1 U) yeast a-glucosidase (Sigma) in water were added and a second incubation of 24 h at 37° C. was carried out. Long incubations at 37° C. (17-24 h) were carried out in 96-well plates which were sealed airtight with broad sticky tape, limiting evaporation to <15%. Next, 200 μL 0.5 mol/L Na2CO3/NaHCO3, pH 10.7, was added, and the fluorescence of the released 4-methylumbelliferone (MU) was measured on a Fluoroskan (Titertek) fluorimeter. Protein was determined as described previously (van Diggelen et al., Clin. Chim. Acta., 187:131-139 (1990)).
5
Evaluation of Yeast α-Glucosidase Inhibitors
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Yeast α-glucosidase, p-nitrophenyl α-d -glucopyranoside (p-NPG), acarbose, p-nitrophenyl phosphate (p-NPP), ursolic acid, ethylenediaminetetraacetic acid (EDTA), ascorbic acid, penicillamine, and 2,2-diphenyl-1-picrylhydrazyl (DPPH) were purchased from Sigma Aldrich (St. Louis, MO, USA). PTP1B (human recombinant) was purchased from Biomol® International, LLP (Plymouth Meeting, PA, USA), and dithiothreitol (DTT) was purchased from Bio-Rad Laboratories (Hercules, CA, USA). A BACE1 FRET assay kit (β-secretase) was purchased from PanVera Corp. (Madison, WI, USA). Peroxynitrite was purchased from Cayman Chemical (Ann Arbor, MI, USA). All other chemicals and solvents were purchased from E. Merck (Darmstadt, Germany), Honeywell Fluka (Morris Plains, NJ, USA), and Sigma-Aldrich, unless otherwise stated.
6
Antidiabetic Potential of Bitter Gourd Varieties
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The fruits of M. charantia var. charantia (MCC) and M. charantia var. muricata (MCM) were bought from the local market in Chengalpet, Tamil Nadu, India. They were taxonomically identified by a botanist and verified by DNA barcoding. Porcine α-amylase and yeast α-glucosidase were bought from Sigma Aldrich, and Acarbose from Bayer AG (Germany).
7
Yeast α-Glucosidase Inhibition Assay
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The enzyme inhibition activity against yeast α-glucosidase (Sigma-Aldrich, USA) were determined using 1 mM of p-nitrophenyl-α-D-glucopyranoside (PNPG) as substrate according to Wan et al.[12 (link)] with minor modifications. In 96 well plate, 30 μl of enzyme solution (0.5 U/ml), 30 μl of 0.1 M sodium phosphate buffer (pH 6.9) and 30 μl of tested inhibitors (mango, mangiferin [MIRA, China], or acarbose [Sigma-Aldrich, USA]) in dimethyl sulfoxide (DMSO) were mixed and incubated at 37°C for 10 min. Next, 30 μl of substrate were added and incubated again at 37°C for 20 min. After incubation, 80 μL of 0.2 μM Na2 CO3 was added to stop the reaction. The absorbance was measured at 405 nm using Anthos Zenyth 200 RT microplate reader (Biochrom, England). All tested inhibitors were analyzed in triplicate. The percent inhibition was calculated by the following formula:
8
Marine Biopolymers for Enzyme Inhibition
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Squid pens, crab shells and shrimp shells were obtained from Shin-Ma Frozen Food Co. (I-Lan, Taiwan) [45 (link)]. Shrimp head powder (SHP) was acquired from Fwu-Sow Industry (Taichun, Taiwan). Demineralized shrimp shell powder (deSSP) and demineralized crab shell powder (deCSP) were prepared according to the previously described methods [45 (link)]. Acarbose, p-nitrophenyl glucopyranoside and enzymes (yeast α-glucosidase, rat α-glucosidase, porcine pancreatic α-amylase, B. subtilis α-amylase, lysozyme, cellulase, bromelain and papain) were obtained from Sigma Chemical Co., St. Louis, MO, USA. The Macro-Prep High S column was obtained from BioRad (Hercules, CA, USA). All other reagents used were of the highest grade available.
9
Yeast α-Glucosidase Inhibition Assay
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The α-glucosidase inhibitory assay was based on the chromogenic method developed by Watanabe et al. (21 (link)), and it was performed using a readily available yeast enzyme. Briefly, yeast α-glucosidase (0.7 U, Sigma-Aldrich Co., St. Louis, MO, USA) was dissolved in 100 mM phosphate buffer (pH 7.0) containing 2 g/L bovine serum albumin and 0.2 g/L NaN3 and used as the enzyme solution. Five mM p-nitrophenyl-α-D-glucopyranoside in the same buffer (pH 7.0) was used as the substrate solution. Fifty μL enzyme solution and 10 μL SYE [5 mg/mL in dimethyl sulfoxide (DMSO)] were mixed in a well, and the absorbance at 405 nm was measured as time zero using a microplate reader. After incubation for 5 min, the substrate solution (50 μL) was added, and the incubation continued for another 5 min at room temperature. The increase in absorbance from the zero time point was then measured. The inhibitory activities of varying concentrations of SYE were expressed as 100 minus the absorbance difference (%) of the test compounds relative to the absorbance change of the negative control (i.e., DMSO used as the test solution). The measurements were performed in triplicate, and the IC50 value (i.e., the concentration of SYE that result in 50% inhibition of maximal activity) was determined.
10
α-Glucosidase Inhibition Assay by Chromogenic Method
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The α-glucosidase inhibitory assay was carried out by the chromogenic method developed by Watanabe et al. (1997 (link)) using a readily available yeast enzyme. Briefly, yeast α-glucosidase (0.7 U, Sigma, St. Louis, MO) was dissolved in 100 mM phosphate buffer (pH 7.0) containing 2 g/L of bovine serum albumin and 0.2 g/L of NaN3 and used as an enzyme solution. p-Nitrophenyl-α-d -glucopyranoside (5 mM) in the same buffer (pH 7.0) was used as a substrate solution. Enzyme solution (50 μL) and 10 μL of sample dissolved in dimethylsulfoxide at a concentration of 5 mg/mL were mixed in a well, and absorbance at 405 nm was measured using a microplate reader. After incubation for 5 min, substrate solution (50 μL) was added and incubated for another 5 min at room temperature. The increase in absorbance from zero time was measured. Inhibitory activity was expressed as 100 minus the relative absorbance difference (%) of the test compounds compared to the absorbance change of the control where the test solution is replaced by carrier solvent. Measurements were performed in triplicate, and IC50 value, i.e., concentration of extracts resulting in 50% inhibition of maximal activity, was determined.
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