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A5168 Sigma

Adenosine Deaminase from bovine spleen

Type IX, ammonium sulfate suspension, 150-200 units/mg protein

Synonym: Adenosine aminohydrolase

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Properties

Related Categories 3.5.x.x Acting on C-N other than peptides, 3.x.x.x Hydrolases, Biochemicals and Reagents, Cell Biology, Enzyme Class Index,
type   Type IX
form   ammonium sulfate suspension
foreign activity   5′-AMP deaminase ≤0.01%
  alkaline phosphatase ≤0.01%
  guanase ≤0.01%
  nucleoside phosphorylase ≤0.1%
storage temp.   2-8°C
Gene Information   cow ... ADA(280712)

Description

Analysis Note

Protein determined by biuret.

Unit Definition

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

Physical form

Suspension in 3.2 M (NH4)2SO4, 0.01 M potassium phosphate, pH 6.0

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.

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.

General description

Molecular weight: 32.5-33 kDa

pI: 4.85

Price and Availability


All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles

Articles

Ammonium Sulfate Suspensions - Technical Note

Note that for an ammonium sulfate suspension, most of the enzyme will be in solid form. It is likely that only negligible amounts of enzyme will be in the ammonium sulfate solution.
Keywords: Enzyme activity

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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