EC Number   |
Application |
Reference |
|---|
    1.2.1.3 | analysis |
a reliable, enzyme-coupled assay for measuring glycerol dehydratase activity in crude-cell extract is developed using 1,2-propanediol as the substrate. In the assay, 1,2-propanediol is converted to propionaldehyde, which is quickly converted to 1-propionic acid by aldehyde dehydrogenase (with the production of NADH) or to 1-propanol by yeast alcohol dehydrogenase (with the consumption of NADH). The change in NADH concentration, as monitored at 340 nm spectrophotometrically, manifested as a straight line for 3 min, from which the glycerol dehydratase activity can be determined. Cells are assumed to have been disintegrated by physical methods (Bead Beater or French Press), not by chemical methods. The assay method should prove to be applicable to recombinant strains developed for the production of 3-hydroxypropionic acid and/or and/or 1,3-propanediol from glycerol |
748353 |
| 1.2.1.3 | analysis |
spectrophotometric assay for the sensitive measurement of the glycerol dehydratase activity with a sub-nanomolar limit of detection. The assay method employs aldehyde dehydrogenase as a reporter enzyme, so the readout of the glycerol dehydratase activity is recorded at 340 nm as an increase in UV absorbance which results from NADH generation accompanied by oxidation of 3-hydroxypropionaldehyde to 3-hydroxypropionic acid. The glycerol dehydratase assay is performed under the reaction conditions where the aldehyde dehydrogenase activity overwhelms the GDHt activity (i.e., 50fold higher activity of aldehyde dehydrogenase relative to glycerol dehydratase activity), affording sensitive detection of glycerol dehydratase with 360 pM limit of detection |
-, 748257 |
| 1.2.1.3 | medicine |
ALDH activity is observed in esophageal cancer tissues |
697569 |
| 1.2.1.3 | medicine |
ALDH activties are significantly higher in liver cancer cells than in normal tissue and might, therefore, be a factor of metabolic changes in low-maturity cancer cells |
686331 |
| 1.2.1.3 | medicine |
ALDH isoenzymes play a major role in the biology and drug resistance of various malignant cells |
724716 |
| 1.2.1.3 | medicine |
breast cancers with ALDH1+ cancer stem cells possess biologically aggressive phenotypes with a tendency leading to poor prognosis |
697114 |
| 1.2.1.3 | medicine |
findings are useful for basic studies about normal erythropoietic differentiation as well as for enabling the employment of ALDH as a red cell marker in polychromatic flow cytometry characterization of bone marrow from patients with aplastic anemia and myelodysplasia |
696996 |
| 1.2.1.3 | medicine |
glyceryl trinitrate is used in the treatment of angina pectoris and cardiac failure, but the rapid onset of glyceryl trinitrate tolerance limits its clinical utility.The majority of the vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of glyceryl trinitrate by ALDH2 plays a minor role in the overall vascular biotransformation |
656837 |
| 1.2.1.3 | medicine |
in human capacitance vessels ALDH2 is s a key enzyme for the biotransformation of the frequently used antianginal drug nitroglycerin |
697845 |
| 1.2.1.3 | medicine |
serum levels of aldehyde dehydrogenase are not significantly higher in patients with gastric cancer in comparison with the healthy group |
697567 |
