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C2624

Sigma-Aldrich

Carbonic Anhydrase from bovine erythrocytes

≥95% (SDS-PAGE), specific activity ≥3,500 W-A units/mg protein, lyophilized powder

Synonym(s):

Carbonic Anhydrase from bovine erythrocytes, Carbonate Dehydratase, Carbonate Hydrolyase

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About This Item

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

biological source

bovine erythrocytes

Quality Level

assay

≥75% protein basis (biuret)
≥95% (SDS-PAGE)

form

lyophilized powder

specific activity

≥3,500 W-A units/mg protein

solubility

deionized water: >10 mg/mL

storage temp.

2-8°C

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Application

Carbonic anhydrase, from bovine erythrocytes, is used to create carbon dioxide capture systems and to research various purification techniques . Carbonic anhydrase is also used to study acid-base regulation in fish and carbonic anhydrase type II deficiency syndrome .

Biochem/physiol Actions

Carbonic Anhydrase is a zinc-containing enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate. One of its main physiological roles is to maintain the acid-base balance in blood and other tissues. Lack of carbonic anhydrase results in carbonic anhydrase type II deficiency syndrome, which is an autosomal recessive disease that causes osteopetrosis, renal tubular acidosis and brain calcifications .

Unit Definition

One Wilbur-Anderson (W-A) unit will cause the pH of a 0.02 M Trizma buffer to drop from 8.3 to 6.3 per min at 0°C. (One W-A unit is essentially equivalent to one Roughton-Booth unit.)

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Nicolas Ghéczy et al.
RSC advances, 10(32), 18655-18676 (2020-05-18)
Enzyme-catalysed cascade reactions in flow-through systems with immobilised enzymes currently are of great interest for exploring their potential for biosynthetic and bioanalytical applications. Basic studies in this field often aim at understanding the stability of the immobilised enzymes and their
Abdur Rauf et al.
Chemistry & biodiversity, 14(6) (2017-02-17)
Plant phenolics are known to display many pharmacological activities. In the current study, eight phenolic compounds, e.g., luteolin 5-O-β-glucoside (1), methyl rosmarinate (2), apigenin (3), vicenin 2 (4), lithospermic acid (5), soyasaponin II (6), rubiadin 3-O-β-primeveroside (7), and 4-(β-d-glucopyranosyloxy)benzyl 3,4-dihydroxybenzoate
Marco Catalano et al.
Analytical chemistry, 92(15), 10822-10829 (2020-07-04)
The availability of reliable methods for the characterization of the binding of small molecule ligands to protein targets is crucially important for drug discovery. We have adapted a method, routinely used for the characterization of monoclonal antibodies (enzyme-linked immunosorbent assay
K M Gilmour et al.
The Journal of experimental biology, 212(Pt 11), 1647-1661 (2009-05-19)
Carbonic anhydrase (CA) is the zinc metalloenzyme that catalyses the reversible reactions of CO(2) with water. CA plays a crucial role in systemic acid-base regulation in fish by providing acid-base equivalents for exchange with the environment. Unlike air-breathing vertebrates, which
Joana da Costa Ores et al.
Chemosphere, 88(2), 255-259 (2012-04-20)
This work presents a study of industrially applicable techniques to obtain a biologically supported carbon dioxide capture system, based on the extraction of carbonic anhydrase from bovine blood. Carbonic anhydrase is a metalloenzyme which catalyzes the reversible hydration of carbon

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