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A1520

Sigma-Aldrich

α-Amylase Inhibitor from Triticum aestivum (wheat seed)

Type I, lyophilized powder

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.77

Biologische Quelle

Triticum estivum

Qualitätsniveau

Typ

Type I

Form

lyophilized powder

Spezifische Aktivität

≥1000 inhibitor U/mg protein (using human salivary α-amylase)
≥200 inhibitor U/mg protein (using porcine pancreatic α-amylase)

Zusammensetzung

Protein, 35-65% biuret

Lagertemp.

−20°C

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Allgemeine Beschreibung

α-Amylases are endoglycosidases, that are classified into glycosyl hydrolase family 13 (1-3).

Anwendung

α-Amylase Inhibitor from Triticum aestivum (wheat seed) has been used to determine its effects on salivary gland (SG) amylase activity. It has also been used to inhibit the activity from the extract from Bemisia tabaci.

Biochem./physiol. Wirkung

α-Amylases can hydrolyze α-(1,4)-D-glycosidic linkages. It participates in the breakdown of starch and glycogen. Inhibiting this enzyme can be used as a strategy to treat dental caries, diabetes, obesity and periodontal diseases.
Competitive inhibitor of human salivary α-amylase. KI = 2.9 nM, compared to a KM of 5.9 mM (calculated per mole of α-1,4-linked maltose residues).

Einheitendefinition

One unit will reduce the activity of two units of α-amylase (A0521) by 50% after pre-incubation at 25 °C.

Physikalische Form

Lyophilized powder containing buffer salts as sodium phosphate.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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A review of alpha-amylase inhibitors on weight loss and glycemic control in pathological state such as obesity and diabetes
Mahmood N
Comparative clinical pathology, 25(6), 1253-1264 (2016)
Partial characterization of alpha-amylase in the salivary glands of Lygus hesperus and L. lineolaris
Zeng F and Cohen AC
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 126(1), 9-16 (2000)
alpha-Amylase inhibitors: a review of raw material and isolated compounds from plant source
Sales PM, et al.
J. Pharm. Pharm. Sci., 15(1), 141-183 (2012)
Demonstration and preliminary characterization of -amylase in the sweetpotato whitefly, Bemisia tabaci (Aleyrodidae: Homoptera)
Cohen AC and Hendrix DL
Comparative Biochemistry and Physiology (1994)
Frauke Schocker et al.
International archives of allergy and immunology, 174(1), 17-25 (2017-09-28)
Little is known about breast milk as a vehicle for tolerance development or sensitization to peanuts very early in life. Thus, well-characterized and highly sensitive detection systems for the reliable determination of peanut allergens in breast milk are mandatory. For

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