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
Sinónimos:
Aldehyde:NAD[P]+ oxidoreductase
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form
lyophilized powder
Quality Level
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.[1] 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.[2] 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.[3]
Aldehyde dehydrogenase (ALDH) is present in the nucleus, cytosol, mitochondria and endoplasmic reticulum of cells.[4]
Application
Biochem/physiol Actions
Aldehyde dehydrogenase from baker′s yeast catalyzes the reduction of pyridine nucleotides by several aldehydes.[2] 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.[7] 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.[8][9]
Unit Definition
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.
Physical form
Contains lactose, potassium phosphate and citrate buffer salts, and mercaptosuccinic acid.
Reconstitution
This enzyme can be dissolved at 0.3 mg/mL in 100 mM Tris-HCl buffer (pH 8.0), containing 0.02% BSA.
Storage Class
11 - Combustible Solids
wgk_germany
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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