D7876
Diamine Oxidase from porcine kidney
≥0.05 unit/mg solid
Synonym(s):
Amine:oxygen oxidoreductase (deaminating) (pyridoxal-containing)
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-613-6
NACRES:
NA.54
MDL number:
Product Name
Diamine Oxidase from porcine kidney, ≥0.05 unit/mg solid
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
Quality Level
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.
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.
Other Notes
One unit will oxidize 1.0 μmole of putrescine per hr at pH 7.2 at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
动植物源性产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Marta Moniente et al.
Food research international (Ottawa, Ont.), 160, 111735-111735 (2022-09-10)
Lentilactobacillus parabuchneri is the main bacteria responsible for the accumulation of histamine in cheese. The goal of this study was to assess the efficiency of potential histamine-degrading microbial strains or, alternatively, the action of the diamine oxidase (DAO) enzyme in
M A Shah et al.
The Biochemical journal, 253(1), 103-107 (1988-07-01)
Pig kidney diamine oxidase (DAO) was found to contain 5% (w/w) natural hexose, 3.25% glucosamine, 2.61% N-acetylglucosamine and 0.25% N-acetylneuraminic acid. The enzyme exhibited strong affinity towards concanavalin A (Con A) with a stoichiometry of 1:4.6. The kinetics of interaction
A PRELIMINARY INVESTIGATION ON A HISTAMINE BIOSENSOR CONSTRUCTED FROM DIAMINE OXIDASE IMMOBILISED ONTO AN OXYGEN PROBE
Gupta N MM, et al.
International Journal of Pharmaceutical Sciences and Research (2018)
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
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
Protocols
To standardize a procedure for the enzymatic assay of Diamine Oxidase.
Related Content
Product Information Sheet
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service