The purification method is proprietary, and testing for other activities, such as alcohol dehydrogenase, is not conducted. The following reference from the Product Information Sheet may be helpful: Bostian, K. A., and Betts, G. F., Rapid purification and properties of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae. Biochemical Journal, 173(3), 773-786 (1978).
A6338
Aldehyde Dehydrogenase, potassium-activated from baker′s yeast (S. cerevisiae)
lyophilized powder, ≥2.0 units/mg protein
Synonym(s):
Aldehyde:NAD[P]+ oxidoreductase
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| Size/SKU | Availability | Price |
|---|---|---|
25 units | Check Cart for Availability | $84.20 |
100 units | Check Cart for Availability | $218.00 |
250 units | Check Cart for Availability | $448.00 |
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-846-3
MDL number:
Specific activity:
≥2.0 units/mg protein
form
lyophilized powder
Quality Segment
specific activity
≥2.0 units/mg protein
mol wt
228 kDa
composition
Protein, ≥5.0% biuret
shipped in
dry ice
storage temp.
−20°C
General description
Aldehyde dehydrogenase is a tetramer and has several different isoforms. The enzyme tested in 0.01 M pyrophosphate buffer shows a sharp optimum around pH 9.3 with acetaldehyde as substrate. Potassium ions and cysteine are essential for the enzyme′s activity. Rubidium or NH4+ can be substituted for K+, and glutathione for cysteine. Lithium, Na+, and Cs+ inhibit the reaction. Aldehyde dehydrogenase is inhibited by propylurea, crotonaldehyde, n-propyl isocyanate, cyclohexyl isocyanate, 1-n-propyl-1-[(4-chlorophenyl)sulphonyl]-3-n-propylurea, and 1-methyl-1-[(4-chlorophenyl)sulphonyl]-3-n-propylurea. The enzyme may be utilized to quantitate aldehydes present in blood.
Aldehyde dehydrogenase (ALDH) is present in the nucleus, cytosol, mitochondria and endoplasmic reticulum of cells.
Application
Biochem/physiol Actions
Aldehyde dehydrogenase from baker′s yeast catalyzes the reduction of pyridine nucleotides by several aldehydes. It catalyzes the oxidation of a wide range of substrates, such as acetaldehyde, formaldehyde, propionaldehyde, n-butylaldehyde, isobutylaldehyde, n-valeraldehyde, caproaldehyde, benzaldehyde, glycoaldehyde, D-glyceraldehyde, malonic semialdehyde, and succinic aldehyde. Aldehyde dehydrogenase is used to study the production of ethanol and isobutanol. Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of nicotinamide adenine dinucleotide (NAD) using alcohol dehydrogenase after preremoval of aldehyde by aldehyde dehydrogenase.
Physical form
Contains lactose, potassium phosphate and citrate buffer salts, and mercaptosuccinic acid.
Preparation Note
This enzyme can be dissolved at 0.3 mg/mL in 100 mM Tris-HCl buffer (pH 8.0), containing 0.02% BSA.
Other Notes
One unit will oxidize 1.0 μmole of acetaldehyde to acetic acid per min at 25 °C at pH 8.0 in the presence of β-NAD+, potassium and thiols.
1 of 1
This Item | |||
|---|---|---|---|
| description lyophilized powder, ≥2.0 units/mg protein | description lyophilized powder, ≥10 units/mg protein | description from yeast | description Aldehyde Dehydrogenase, Yeast, CAS 9028-88-0, is a native aldehyde dehydrogenase from yeast that catalyzes the oxidation of acetaldehyde to acetic acid. |
| specific activity ≥2.0 units/mg protein | specific activity ≥10 units/mg protein | specific activity ~20 units/mg protein (At 25 °C with acetaldehyde as the substrate.) | specific activity ≥19 units/mg protein |
| form lyophilized powder | form lyophilized powder | form lyophilized | form lyophilized solid |
| mol wt 228 kDa | mol wt - | mol wt - | mol wt - |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| shipped in dry ice | shipped in - | shipped in - | shipped in ambient |
| Quality Level 200 | Quality Level 200 | Quality Level - | Quality Level 100 |
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Re A6338...how was the enzyme purified, and is it confirmed to be free of other activities, e.g. alcohol dehydrogenase?
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