Human salivary α amylase

Manufactured by Merck Group

Sourced in United States

Human salivary α-amylase is an enzyme found in human saliva. It is responsible for the initial breakdown of complex carbohydrates, such as starch, into smaller sugar molecules. This enzyme plays a crucial role in the digestive process.

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Lab products found in correlation

Dimethyl sulfoxide (dmso), by Merck Group (4 mentions) Methanol, by Merck Group (4 mentions) Acetonitrile, by Merck Group (4 mentions) Acarbose, by Merck Group (3 mentions) Formic acid, by Merck Group (3 mentions) α glucosidase, by Merck Group (2 mentions) Mes sds running buffer, by Thermo Fisher Scientific (2 mentions) Instantblue protein stain, by Abcam (2 mentions) Flamingo fluorescent protein stain, by Bio-Rad (2 mentions) Pierce glycoprotein staining kit, by Thermo Fisher Scientific (2 mentions) Bovine liver glycogen, by Merck Group (2 mentions) Chemidoc mp imaging system, by Bio-Rad (2 mentions) 2 2 diphenyl 1 picrylhydrazyl (dpph), by Merck Group (2 mentions) Sodium potassium tartrate, by Merck Group (1 mentions) Glutathione (gsh), by Merck Group (1 mentions) Dinitrosalicylic acid dns, by Merck Group (1 mentions) Porcine pancreatic α amylase type 6 b, by Merck Group (1 mentions) Slide a lyzer 10 k mwco dialysis cassette, by Thermo Fisher Scientific (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Horse myoglobin, by Merck Group (1 mentions)

Spelling variants of this product

α-amylase (451 citations) Salivary α-amylase (7 citations) Salivary amylase (5 citations) Human α-amylase (5 citations) Human salivary α-amylase type IX-A (2 citations)

11 protocols using human salivary α amylase

Algae Extract Anti-Diabetic Potential

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Algae extract, commercially available under the trade name Gdue™ (Lot. N. 201400566), was provided by Aesculapius (Brescia, Italy). The extract was prepared from the dried thallus of Ascophyllum nodosum and Fucus vesiculosus, using a proprietary hot-water extraction process, followed by a series of filtration and ultrafiltration processes, and completed by spray-drying. Alginates and part of salts were removed during the process. The extract constituted a whole plant extract that contained plant polyphenols (35.5%, as indicated in the certificate of analysis of the commercial product), in addition to the algal polysaccharides (fibers) and minerals (iodine content <300 mg/kg).
Starch potato, dipotassium hydrogen phosphate (K₂HPO₄), potassium dihydrogen phosphate (KH₂PO₄), sodium potassium tartrate, sodium hydroxide (NaOH), sodium chloride (NaCl), glutathione, human salivary α-amylase, α-glucosidase, acarbose, p-nitrophenyl-α-d-glucopyranoside (PNP-Gluc), and dinitrosalicylic acid (DNS), were obtained from Sigma Aldrich (St. Louis, MO, USA).

Gabbia D., Dall’Acqua S., Di Gangi I.M., Bogialli S., Caputi V., Albertoni L., Marsilio I., Paccagnella N., Carrara M., Giron M.C, & De Martin S. (2017). The Phytocomplex from Fucus vesiculosus and Ascophyllum nodosum Controls Postprandial Plasma Glucose Levels: An In Vitro and In Vivo Study in a Mouse Model of NASH. Marine Drugs, 15(2), 41.

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Enzyme Inhibition by Tannins

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Porcine pancreatic α-amylase (Type VI-B), human salivary α-amylase, acarbose, and the hydrolysable tannin from Chinese natural gallnuts were purchased from Sigma-Aldrich Co. The condensed tannin from Acacia mearnsii bark was purchased from Labsynth, Brazil.

Kato C.G., Gonçalves G.D., Peralta R.A., Seixas F.A., de Sá-Nakanishi A.B., Bracht L., Comar J.F., Bracht A, & Peralta R.M. (2017). Inhibition of α-Amylases by Condensed and Hydrolysable Tannins: Focus on Kinetics and Hypoglycemic Actions. Enzyme Research, 2017, 5724902.

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Extraction and Purification of Salivary Proteins

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BSA, horse myoglobin, human salivary α-amylase, and protein A from Staphylococcus aureus were obtained from Sigma-Aldrich. An aliquot of human saliva was centrifuged at 2000 g for 15 min, and the supernatant tested at various concentrations in the p53R assay. To extract PRPs, equal volumes of saliva supernatant and 10% (w/v) TCA were mixed and centrifuged at 18000 × g for 10 min at 4°C to remove TCA-insoluble material (adapted from (Robbins et al., 1987 )). The PRP-enriched supernatant was diluted 1:5 in DMEM containing 20 mM HEPES, without FBS or antibiotics. The remaining TCA was neutralized by adding 1 M NaOH drop-wise until the color of the phenol red-containing medium changed. Using a Slide-A-Lyzer 10 K MWCO dialysis cassette (Thermo Scientific), the PRP solution was dialyzed against a 300× excess volume of DPBS initially for 2 h at RT, for another 2 h at RT after changing the dialysate, and finally overnight at 4° C after changing the dialysate again. Graded concentrations of the PRP solution were tested in the p53R assay after TCA extraction, neutralization, and dialysis.

Hossain M.Z., Patel K, & Kern S.E. (2014). Salivary α-amylase, serum albumin, and myoglobin protect against DNA-damaging activities of ingested dietary agents in vitro. Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association, 70, 114-119.

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Enzyme Inhibition Assay Protocol

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All of the reagents including α-glucosidase, dimethyl sulfoxide (DMSO), potassium hydroxide (KOH), phosphate buffer, p-nitrophenyl-glucopyranoside (p-NPG), acarbose, phosphoric acid (H₃PO₄), human salivary α-amylase, 2-chloro-4-nitrophenyl-maltotrioside (CNP-G3), tris-HCl, porcine pancreas lipase, p-nitrophenyl butyrate (p-NPB), methanol, orlistat, acetonitrile, deuterated methanol (MeOH-d₄), deuterated chloroform (CHCl₃-d), eriodictyol, naringenin, and quercetin were purchased from Sigma Aldrich. The solvents used for extraction (ethanol—EtOH), HPLC (acetonitrile—MeCN), and LC–MS (MeCN and water—H₂O) analyses were purchased from Merck. The ultra-pure water used for the HPLC analysis was from an in-house Milli-Q system.

Uddin S., Brooks P.R, & Tran T.D. (2022). Chemical Characterization, α-Glucosidase, α-Amylase and Lipase Inhibitory Properties of the Australian Honey Bee Propolis. Foods, 11(13), 1964.

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Characterization of Intestinal Digestion Compounds

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All 36 investigated drugs and the two standard solutions (thiorphan and S-acetylthiorphan) were commercially purchased from Sigma-Aldrich (St. Louis, MO, United States), and the detailed information about these compounds is listed in Supplementary Table S1. Acetonitrile, methanol, dimethyl sulfoxide, formic acid, and ammonium acetate were HPLC grade, and along with KCl, KH₂PO₄, NaHCO₃, NaCl, MgCl₂(H2O)₆, (NH₄)₂CO₃, CaCl₂(H₂O)₂, L-cysteine, ethyl acetate, HCl, and NaOH were bought from Merck (Darmstadt, Germany). Bryant and Burkey Medium (BB), de Man Rogosa Sharpe (MRS) broth, glycerol, human salivary α-amylase, porcine pepsin, rabbit gastric extract for gastric lipase, bovine bile, and porcine pancreatin were purchased from Sigma-Aldrich (St. Louis, MO, United States). Modified Gifu anaerobic medium (mGAM) broth was purchased from HyServe GmbH and Co., KG (Germany). Ultrapure water used throughout the study was prepared by a Milli-Q water purification system (Millipore, Molsheim, France).

Li B., Kwok L.Y., Wang D., Li L., Guo S, & Chen Y. (2023). Integrating metabolomics, bionics, and culturomics to study probiotics-driven drug metabolism. Frontiers in Pharmacology, 14, 1047863.

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Enzymatic Digestion of Amylase in Fruits

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Mature fruits of A. integer were obtained from the Central Market, Sibu, Sarawak, Malaysia, and were transported immediately to the laboratory and stored at 4°C until further use. Human salivary α-amylase was purchased from Sigma-Aldrich. All chemicals used in this study were of analytical grade unless specified otherwise. Lactobacillus acidophilus DSM 20079, Lactobacillus casei DSM 20011, and Escherichia coli DSM 1103 were purchased from Leibniz-Institut DSMZ GmbH (Braunschweig, Germany). All stock cultures were maintained in sterile glycerol (30% v/v) at −20°C.

Wong J.C., Hii S.L, & Koh C.C. (2021). Isolation of Prebiotics from Artocarpus integer's Seed. International Journal of Food Science, 2021, 9940078.

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SARS-CoV-2 Detection by MALDI-ToF Mass Spectrometry

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Human serum antibodies IgA (I4036), IgG (I4506) and IgM (I8260) (Sigma-Aldrich, St. Louis, MO) were reduced with 1 M DTT for 10 min to a final concentration of 3 pmol of each antibody on the plate. Human salivary α-amylase (A1031, Sigma-Aldrich, St. Louis, MO) was prepared at 100 pmol/μl in LC-MS grade H₂O, 1 μL of which was spotted. Preparation of positive and negative controls for MALDI-ToF analysis followed closely to that of gargle samples. The negative control, consisting of pooled human saliva (pre-COVID-19) collected before November 2019 (Lee Biosolutions, Maryland Heights, MO), was prepared by spiking 500 µL of the thawed stock into 10 mL of water in a 50 mL tube. From here, the control was filtered and processed following the gargle sample procedure. The positive control (heat inactivated SARS-CoV-2) was obtained from BEI Resources (NR-52286). Briefly, this standard was a heat inactivated, clarified, and diluted cell lysate and supernatant from Vero E6 cells infected with SARS-CoV-2. This sample (225 µL) was treated with 4X v/v of chilled acetone (900 µL) and incubated overnight at −20 °C followed by centrifugation at 10,000 × g for 15 min at 4 °C. The pellet was completely dissolved in 25 µL of the reconstitution buffer.

Chivte P., LaCasse Z., Seethi V.D., Bharti P., Bland J., Kadkol S.S, & Gaillard E.R. (2021). MALDI-ToF protein profiling as a potential rapid diagnostic platform for COVID-19. Journal of Mass Spectrometry and Advances in the Clinical Lab, 21, 31-41.

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Ubiquitin Conjugation Assay with Glycogen

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Reactions (20 μl) contained 500 nM His₆‐UBE1, 2 μM UBE2L3, 2 μM HOIL‐1, 10 μM Cy5‐ubiquitin (South Bay Bio) and 10 mg/ml bovine liver glycogen (Sigma) in phosphate buffered saline pH 7.4 containing 0.5 mM TCEP and 5 mM Mg²⁺‐ATP. Reactions were incubated at 37°C for 1 h with gentle mixing. Where indicated, reactions were then incubated in the presence of 50 μg/ml (~0.1 units) human salivary α‐amylase (Sigma) or 1.5 M hydroxylamine for a further 60 min at 37°C. Reactions were stopped by adding NuPAGE LDS sample loading buffer supplemented with 50 mM DTT, and denatured at room temperature for 10 min. Reaction products were separated by gel electrophoresis on 4–12% Bis–Tris gradient gels using MES SDS running buffer (Invitrogen) and stained with Flamingo fluorescent protein stain (Bio‐Rad). Visualisation of the fluorescent signals was performed using the ChemiDoc MP Imaging System (Bio‐Rad) and ImageJ software (Schneider et al, 2012 (link)). In the case of assays using glycogen as substrate, these gels were then stained with periodic acid‐Schiff stain using the Pierce Glycoprotein Staining Kit (Thermo Scientific) and Coomassie stained with InstantBlue Protein Stain (Expedeon).

Kelsall I.R., McCrory E.H., Xu Y., Scudamore C.L., Nanda S.K., Mancebo‐Gamella P., Wood N.T., Knebel A., Matthews S.J, & Cohen P. (2022). HOIL‐1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation. The EMBO Journal, 41(8), e109700.

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In Vitro Ubiquitination Assay with Glycogen

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Reactions (20 μL) contained 500 nM His 6 -UBE1, 2 μM UBE2L3, 2 μM HOIL-1, 10 μM Cy5-ubiquitin (South Bay Bio) and 10 mg/mL bovine liver glycogen (Sigma) in Phosphate Buffered Saline pH 7.4 containing 0.5 mM TCEP and 5 mM Mg 2+ -ATP. Reactions were incubated at 37°C for 1 h with gentle mixing. Where indicated, reactions were then incubated in the presence of 50 μg/mL (~0.1 units) human salivary α-amylase (Sigma) or 1.5 M hydroxylamine for a further 60 min at 37°C. Reactions were stopped by adding NuPAGE LDS sample loading buffer supplemented with 50 mM DTT, and denatured at room temperature for 10 min. Reaction products were separated by gel electrophoresis on 4-12% Bis-Tris gradient gels using MES SDS running buffer (Invitrogen) and stained with Flamingo fluorescent protein stain (Bio-Rad). Visualisation of the fluorescent signals was performed using the ChemiDoc MP Imaging System (Bio-Rad) and ImageJ software. In the case of assays using glycogen as substrate, these gels were then stained with Periodic acid-Schiff stain using the Pierce Glycoprotein Staining Kit (Thermo Scientific) and Coomassie stained with InstantBlue Protein Stain (Expedeon).

Kelsall I.R., McCrory E.H., Xu Y., Scudamore C.L., Nanda S.K., Mancebo‐Gamella P., Wood N.T., Knebel A., Matthews S., & Cohen P. (2021). HOIL-1-catalysed ubiquitylation of unbranched glucosaccharides and its activation by ubiquitin oligomers.

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Antioxidant Evaluation of Tetrastigma hemsleyanum

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Fresh Tetrastigma hemsleyanum roots were purchased from Jiangxi Shangrao Red Sun Agricultural Development Co., Ltd. (Nanchang, China). Pepsin, bile salts, and pancreatin were obtained from Aladdin Co. Ltd. (Shanghai, China). Human salivary a-amylase, DPPH, and DMSO were purchased from Sigma-Aldrich Co. (St. Louis, MO, USA). Methanol, acetonitrile, formic acid, and other solvents and chemical agents were obtained from Merck (Darmstadt, Germany). Water was purified in-house by a Milli-Q system (Bedford, MA, USA). The superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), total antioxidant capacity (T-AOC), reduced glutathione (GSH), and malondialdehyde (MDA) kits were purchased from Nanjing Jiancheng Bioengineering Company (Nanjing, China).

Sun Y., Guo F., Peng X., Cheng K., Xiao L., Zhang H., Li H., Jiang L, & Deng Z. (2021). Metabolism of Phenolics of Tetrastigma hemsleyanum Roots under In Vitro Digestion and Colonic Fermentation as Well as Their In Vivo Antioxidant Activity in Rats. Foods, 10(9), 2123.

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