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Merck

A5043

Adenosine Deaminase from bovine spleen

Type X, buffered aqueous glycerol solution, ≥130 units/mg protein

Synonym(s):

ADA, adenosine aminohydrolase, Adenosine aminohydrolase

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
MDL number:
Specific activity:
≥130 units/mg protein
Biological source:
bovine spleen
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biological source

bovine spleen

Quality Level

type

Type X

form

buffered aqueous glycerol solution

specific activity

≥130 units/mg protein

mol wt

32.5-33 kDa

cation traces

NH4+: ≤10 μg/mg protein

UniProt accession no.

foreign activity

alkaline phosphatase ≤0.01%, guanase ≤0.01%, nucleoside phosphorylase ≤0.1%

storage temp.

2-8°C

Gene Information

cow ... ADA(280712)

General description

Molecular weight: 32.5-33 kDa

pI: 4.85

Application

Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays . Adenosine deaminase is a potential target for treatments of combined immunodeficiency disease.
Adenosine Deaminase from bovine spleen has been used in the immobilization on biostrip for stability and catalytic studies.

Biochem/physiol Actions

Adenosine deaminase is a purine catabolic enzyme which catalyzes the deamination of adenosine and 2′-deoxyadenosine with approximately equal specificity. It is ubiquitous in mammalian tissue, and deficiency in adenosine deaminase has been associated with severe combined immunodeficiency disease.

Physical form

Solution in 50% glycerol, 5 mM potassium phosphate, pH 6.0

Analysis Note

Protein determined by biuret.

Other Notes

One unit will deaminate 1.0 μmole of adenosine to inosine per min at pH 7.5 at 25 °C.


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Storage Class

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable



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Adenosine reagent-free detection by co-immobilization of adenosine deaminase and phenol red on an optical biostrip
Bartzoka F, et al.
Biotechnology Journal, 10(1), 136-142 (2015)
Ying Cheng et al.
Diabetes, 59(1), 17-25 (2009-10-17)
White adipose tissue (WAT) and brown adipose tissue (BAT) play distinct roles in adaptation to changes in nutrient availability, with WAT serving as an energy store and BAT regulating thermogenesis. We previously showed that mice maintained on a leucine-deficient diet
Yeon-Mi Lee et al.
Biophysical chemistry, 172, 18-25 (2013-01-22)
Human ADAR1, which has two left-handed Z-DNA binding domains, preferentially binds Z-DNA rather than B-DNA with a high binding affinity. Z-DNA can be induced in long genomic DNA by Z-DNA binding proteins through the formation of two B-Z junctions with