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B2170

Sigma-Aldrich

Bromoperoxidase from Corallina officinalis

lyophilized powder, ≥100 units/mg protein (Lowry)

Synonym(s):

BCB, Bromide Peroxidase

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥100 units/mg protein (Lowry)

composition

Protein, ~10%

solubility

water, ethanol: soluble, violet

foreign activity

Chloroperoxidase <1%

storage temp.

−20°C

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Application

Bromoperoxidase from Corallina officinalis may be used for staining brain tissue, nuclei, plant chromosomes, reticulocytes, platelets and reticulated red cells. It may be used for the detection of biochemical molecules and the BCB enzyme assay. The BCB assay is also used industrially in optical data storage.

Biochem/physiol Actions

Bromoperoxidase from Corallina officinalis is a phenoxazine dye. The brilliant cresyl blue (BCB) test determines the activity of glucose-6-phosphate dehydrogenase (G6PDH). The activity of this enzyme is greatest in growing oocytes and declines as oocytes mature. It stains reticulocytes and trichomonads. Bromoperoxidase contains a significant amount of nonheme iron. It is activated by vanadate ions. Maximal activity is achieved with stoichiometric vanadium incorporation .

Unit Definition

One unit will catalyze the conversion of 1.0 μmole of monochlorodimedon to monobromochlorodimedon per min at pH 6.4 at 25 °C.

Physical form

Partially purified, lyophilized powder containing MES buffer salts

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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H Yu et al.
Biochemical and biophysical research communications, 160(1), 87-92 (1989-04-14)
A nonheme bromoperoxidase has been purified to homogeneity from the red seaweed Corallina officinalis. Like the corresponding enzyme previously reported from C. pilulifera, this bromoperoxidase contains a significant amount of nonheme iron. However, it is vanadate ion and not iron

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