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Key Documents

D7876

Sigma-Aldrich

Diamine Oxidase from porcine kidney

≥0.05 unit/mg solid

Synonyme(s) :

Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing)

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Porcine kidney

Niveau de qualité

Forme

solid

Activité spécifique

≥0.05 unit/mg solid

Poids mol.

170 kDa

Solubilité

100 mM sodium phosphate buffer, pH 7.2: soluble 10 mg/mL

Activité étrangère

monoamine oxidase (benzylamine substrate) ≤1%

Température de stockage

−20°C

Description générale

Diamine oxidase from porcine kidney is a homodimer consisting of two equal subunits with a molecular weight of 87 kDa each. Each subunit contains one molecule of pyridoxal phosphate and one atom of copper. The molecular mass of the enzyme is found to be 170 kDa. The enzyme is a glycoprotein containing 5% hexose, 3.3% glucosamine, 2.6% N-acetylglucosamine, and 0.25% N-acetylneuraminic acid. The enzyme exhibits a high affinity for concanavalin A. Optimum pH with cadverine and histamine as substrates is found to be 6.3-7.4.

Application

Diamine Oxidase from porcine kidney has been used in the construction of histamine biosensor.
Diamine oxidase from porcine kidney has been used in a study to investigate a luminescence-based test for determining ornithine decarboxylase activity. Diamine oxidase from porcine kidney has also been used in a study to investigate N-linked oligosaccharide structures in diamine oxidase.

Actions biochimiques/physiologiques

Diamine Oxidase catalyzes the oxidation of monoamines, diamines, and histamine to aldehydes, ammonia, and hydrogen peroxide. The enzyme is classified as a copper amine oxidase and it is a key enzyme in nitrogen metabolism. Diamine oxidase is inhibited by diethyldithiocarbamate, phenylhydrazine, semicarbazide, cyanide, isonicotinic acid hydrazide.

Définition de l'unité

One unit will oxidize 1.0 μmole of putrescine per hr at pH 7.2 at 37 °C.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Y Huang et al.
Carbohydrate research, 323(1-4), 111-125 (2000-04-27)
Structures of the N-linked glycans released from porcine kidney diamine oxidase (DAO) were characterized utilizing various analytical techniques, including matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF-MS), high-performance capillary electrophoresis (HPCE), and high-pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD). The
Diamine oxidase and catalase are expressed in the same cells but are present in different subcellular compartments in porcine kidney.
H G Schwelberger et al.
Inflammation research : official journal of the European Histamine Research Society ... [et al.], 48 Suppl 1, S81-S82 (1999-06-01)
A PRELIMINARY INVESTIGATION ON A HISTAMINE BIOSENSOR CONSTRUCTED FROM DIAMINE OXIDASE IMMOBILISED ONTO AN OXYGEN PROBE
The Enzymes (1970)
HISTAMINE BIOSENSOR: A REVIEW
NorazlinaOthman F, et al.
The Malaysian Journal of Analytical Sciences (2006)
Y Wang et al.
Analytical biochemistry, 287(2), 299-302 (2000-12-09)
A sensitive chemiluminescence-based method for the assay of ornithine decarboxylase (ODC) has been developed. This method, which permits the detection of putrescine (the product of ODC) at a picomolar range, can be used to determine ODC activity in cellular extracts.

Protocoles

To standardize a procedure for the enzymatic assay of Diamine Oxidase.

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