Yes, this product does contain (NH4)2SO4. The concentration is considered proprietary.
B0390
Bilirubin Oxidase from Myrothecium verrucaria
lyophilized powder, 15-65 units/mg protein
Synonym(s):
MvBOx, Bilirubin:oxygen oxidoreductase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Pricing and availability is not currently available.
Recommended Products
biological source
fungus (Myrothecium verrucaria)
Quality Level
form
lyophilized powder
specific activity
15-65 units/mg protein
composition
Protein, ≥15% biuret
storage condition
(Keep container tightly closed in a dry and well-ventilated place.)
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
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sustainability
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technique(s)
toxicology assay: suitable
greener alternative category
, Enabling
shipped in
dry ice
storage temp.
−20°C
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General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biofuel cell research. For more information see the article in biofiles.
Bilirubin oxidase (BOD) belongs to the subclass of the multicopper oxidase family.[1][2] It is usually found in fungi.[2]Bilirubin Oxidase is composed of three cupredoxin-like domains that result in two active sites formed by four copper ions.[3] Research area: Apoptosis
Bilirubin oxidase (BOD) belongs to the subclass of the multicopper oxidase family.[1][2] It is usually found in fungi.[2]Bilirubin Oxidase is composed of three cupredoxin-like domains that result in two active sites formed by four copper ions.[3] Research area: Apoptosis
Application
Biochem/physiol Actions
Bilirubin oxidase (BOD) is a multicopper oxidase that catalyzes the oxidation of bilirubin to biliverdin. Oxygen is the electron acceptor and is reduced to water. The enzyme is used for diagnostic analysis of bilirubin in serum during medical examinations of the serum. It has also been used as an enzymatic catalyst for the cathode of biofuel cells that work under neutral conditions. It is a monomeric protein with a molecular mass of 60 kDa and high reactivity at neutral pH.[8] BOD participates in porphyrin and chlorophyll metabolism.[7]
Bilirubin oxidase (BOD) is capable of oxidizing laccase substrates.[2]
Unit Definition
One unit will oxidize 1.0 μmole of bilirubin per min at pH 8.4 at 37 °C.
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Product No.
Description
Pricing
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Kimihiko Mizutani et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 66(Pt 7), 765-770 (2010-07-08)
Bilirubin oxidase (BOD), a multicopper oxidase found in Myrothecium verrucaria, catalyzes the oxidation of bilirubin to biliverdin. Oxygen is the electron acceptor and is reduced to water. BOD is used for diagnostic analysis of bilirubin in serum and has attracted
A'edah Abu-Bakar et al.
Toxicology and applied pharmacology, 257(1), 14-22 (2011-08-30)
We have previously shown that bilirubin (BR), a breakdown product of haem, is a strong inhibitor and a high affinity substrate of the mouse cytochrome P450 2A5 (CYP2A5). The antioxidant BR, which is cytotoxic at high concentrations, is potentially useful
Luciano Dos Santos et al.
Physical chemistry chemical physics : PCCP, 12(42), 13962-13974 (2010-09-21)
The 'blue copper' enzyme bilirubin oxidase from Myrothecium verrucaria shows significantly enhanced adsorption on a pyrolytic graphite 'edge' (PGE) electrode that has been covalently modified with naphthyl-2-carboxylate functionalities by diazonium coupling. Modified electrodes coated with bilirubin oxidase show electrocatalytic voltammograms
Shannon J Little et al.
Chemical communications (Cambridge, England), 47(31), 8886-8888 (2011-06-16)
A novel bioelectrode system has been prepared in which an enzyme and a conducting polymer hydrogel are combined in a nanostructured scaffold. The latter consists of fibres of carbon NanoWeb, grown by chemical vapour deposition onto reticulated vitreous carbon (RVC).
Franziska Wegerich et al.
Langmuir : the ACS journal of surfaces and colloids, 27(7), 4202-4211 (2011-03-16)
Here, we report on cytochrome c/bilirubin oxidase multilayer electrodes with different cytochrome c (cyt c) forms including mutant forms of human cyt c, which exhibit different reaction rates with bilirubin oxidase (BOD) in solution. The multilayer formation via the layer-by-layer
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