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Human α amylase

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Sourced in Spain, United States

Human α-amylase is an enzyme that catalyzes the hydrolysis of starch, glycogen, and related polysaccharides. It is involved in the breakdown of complex carbohydrates into smaller, more easily digestible units.

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Lab products found in correlation

Porcine pancreatin, by Merck Group (1 mentions) Porcine bile, by Merck Group (1 mentions) Water purification system, by Merck Group (1 mentions) N n dimethylformamide (dmf), by Scharlab (1 mentions) Porcine pepsin, by Merck Group (1 mentions) Furimazine, by Promega (1 mentions) Tacrolimus, by Merck Group (1 mentions) Rapamycin, by Merck Group (1 mentions) Human serum albumin (hsa), by Merck Group (1 mentions) Optiplate 96 hs, by PerkinElmer (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Bovine bile extract, by Merck Group (1 mentions) Nh4 2co3, by Merck Group (1 mentions) Pepsin from porcine gastric mucosa, by Merck Group (1 mentions) Mgcl2 h2o 6, by Merck Group (1 mentions) Kreon 10 000 lu, by Viatris (1 mentions) Nahco3, by Merck Group (1 mentions) Kh2po4, by Merck Group (1 mentions) Na2co3, by Merck Group (1 mentions) Sodium chloride (nacl), by Merck Group (1 mentions)

Spelling variants of this product

α-amylase (451 citations) Human salivary α-amylase (11 citations) α-amylase from human saliva (8 citations) Human saliva α-amylase (2 citations) Human salivary α-amylase type IX-A (2 citations) α‐amylase from human pancreas (2 citations)

5 protocols using human α amylase

1

Chlorophyll Extraction and Analysis Protocol

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Human α-amylase, porcine
pepsin, porcine bile, porcine pancreatin, salts, and the chemicals
needed for enzymatic determinations were supplied by Sigma-Aldrich
Chemical Co. (Madrid, Spain). Gastric lipase (RGE15) was provided
by Lipolytech (Marseille, France). high performance liquid chromatography
(HPLC)-grade solvents (acetone, methanol) were supplied by VWR BDH
Chemicals (Radnor), except for N,N-dimethylformamide (DMF), which was supplied by Scharlab (Barcelona,
Spain). The purified water was obtained from a Milli-Q water purification
system (Millipore, Milford, MA). Chlorophyll a and b and pheophytin a were purchased from
Sigma-Aldrich Chemical Co., and chlorin e4 and rhodin g7 were acquired from Frontier Sci (Utah). The rest of chlorophyll
standards were laboratory-produced following established protocols.31 (link),32 (link)
Viera I., Herrera M, & Roca M. (2021). In Vitro Bioaccessibility Protocol for Chlorophylls. Journal of Agricultural and Food Chemistry, 69(31), 8777-8786.
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2

Luminescent Protein Assay Protocol

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Rapamycin, tacrolimus, human α-amylase, human serum albumin, and BSA were purchased from Sigma-Aldrich. NanoLuc substrate Furimazine was purchased from Promega. The luciferase assay plate OptiPlate-96 HS were purchased from PerkinElmer.
Guo Z., Parakra R.D., Xiong Y., Johnston W.A., Walden P., Edwardraja S., Moradi S.V., Ungerer J.P., Ai H.W., Phillips J.J, & Alexandrov K. (2022). Engineering and exploiting synthetic allostery of NanoLuc luciferase. Nature Communications, 13, 789.
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3

In Vitro Digestive Fluid Preparation

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The simulated digestive fluids to conduct in vitro digestions were prepared with KCl, KH2PO4, NaCl, NaHCO3, MgCl2 (H2O)6, (NH4)2CO3, CaCl2, human α-amylase (1000–3000 U/mg protein), pepsin from porcine gastric mucosa ( ≥ 2500 U/mg protein) and bovine bile extract, all of which were obtained from Sigma-Aldrich Chemical Company (St Louis, MO, USA). The pancreatic enzyme supplements came from Kreon 10,000 LU (Mylan, Canonsburg, PA, USA). For the analytical determinations, Triton-X 100%, trichloroacetic acid (TCA), hexane, Folin-Ciocalteu reagent, Na2CO3, gallic acid (GA), trolox (TX) and the analytical standards were acquired from Sigma-Aldrich Chemical Company (St Louis, MO, USA). Ethanol (95% v/v for analysis), NaOH and HCl, were from AppliChem Panreac (Barcelona, Spain).
Calvo-Lerma J., Paz-Yépez C., Asensio-Grau A., Heredia A, & Andrés A. (2020). Impact of Processing and Intestinal Conditions on in Vitro Digestion of Chia (Salvia hispanica) Seeds and Derivatives. Foods, 9(3), 290.
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4

Glycogenin-1 Expression in Myoblasts and Muscle Tissue

Cited 1 time
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Expression of glycogenin-1 in myoblast cell culture from patient A-1 and frozen muscle tissue from patients B-1, C-1, and C-2 were explored by Western blot with monoclonal antibodies against human glycogenin-1 N-terminal 1:500 (Abnova, Taipei, Taiwan) with or without α-amylase treatment as previously described.7 (link) For this purpose, samples were treated with 10 µg/mL human α-amylase (Sigma-Aldrich, St. Louis, MO) for 1 hour at 37°C to remove sugar residues of the large glycogen molecules. Protein extracts were separated onto 10% Mini-PROTEAN TGX precast gels (Bio-Rad Laboratories, Marnes-la-Coquette, France). Immunoblots were visualized by Immobilon Western Chemiluminescent HRP Substrate (Millipore, Guyancourt, France) on a G-Box system using GeneSnap software (Ozyme, Montigny-le-Bretonneux, France). The glucosylated form of glycogenin-1 differs in size by approximately 1 kDa compared with the α-amylase–treated control.
Ben Yaou R., Hubert A., Nelson I., Dahlqvist J.R., Gaist D., Streichenberger N., Beuvin M., Krahn M., Petiot P., Parisot F., Michel F., Malfatti E., Romero N., Carlier R.Y., Eymard B., Labrune P., Duno M., Krag T., Cerino M., Bartoli M., Bonne G., Vissing J., Laforet P, & Petit F.M. (2017). Clinical heterogeneity and phenotype/genotype findings in 5 families with GYG1 deficiency. Neurology: Genetics, 3(6), e208.
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5

Quantitative Saliva-based α-amylase Assay

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The saliva samples were diluted with buffer containing 20 mM Tris pH 7.2 and 100 mM NaCl to 1:25 folds. The assays were performed in 200 µl formulated assay buffer containing 1 mM CDTA, 0.5% Tergitol NP-40, 0.05% Antifoam 204, 150 mM KCl, 100 mM MES, pH 6.0, 1 mM DTT, and 35 mM thiourea in the presence of 1 µl diluted serum sample, 30 µM substrate 8pyDTZ and 1 nM of LumiLuc based protein sensor. The mixture was first incubated at 25 °C for 30 min without substrate. Upon addition of substrate the change of luminescence signal 520–545 nm was monitored with TECAN plater reader SPARK. The signals then were used to determine α-amylase concentration by correlating it with the calibration curve. The calibration curve was obtained by titration of the sensors with the known amount of human α-amylase (Sigma-Aldrich).
Guo Z., Parakra R.D., Xiong Y., Johnston W.A., Walden P., Edwardraja S., Moradi S.V., Ungerer J.P., Ai H.W., Phillips J.J, & Alexandrov K. (2022). Engineering and exploiting synthetic allostery of NanoLuc luciferase. Nature Communications, 13, 789.
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