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D7876

Sigma-Aldrich

Diamine Oxidase from porcine kidney

≥0.05 unit/mg solid

Sinónimos:

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

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About This Item

Número de CAS:
9001-53-0
Comisión internacional de enzimas:
1.4.3.22 (BRENDA, IUBMB)
EC Number:
232-613-6
MDL number:
MFCD00130946
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine kidney

form

solid

specific activity

≥0.05 unit/mg solid

mol wt

170 kDa

solubility

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

foreign activity

monoamine oxidase (benzylamine substrate) ≤1%

storage temp.

−20°C

General description

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.

Biochem/physiol Actions

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.

Unit Definition

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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 Rinaldi et al.
Preparative biochemistry, 12(1), 11-28 (1982-01-01)
Several methods for the isolation of apparently homogeneous pig kidney diamine oxidase have been reported in recent years (1-7), but these procedures allow to obtain only little amounts of material making very difficult the study of the molecular properties of
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
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.
A PRELIMINARY INVESTIGATION ON A HISTAMINE BIOSENSOR CONSTRUCTED FROM DIAMINE OXIDASE IMMOBILISED ONTO AN OXYGEN PROBE
The Enzymes (1970)
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Protocolos

Enzymatic Assay of Diamine Oxidase (E.C. No. 1.4.3.22)

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

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