Sir, Ethanol, the intoxicant that has plagued civilization down the ages, is metabolized into acetaldehyde by the enzyme alcohol dehydro-genase. In this connection, a medical student recently posed a humorous but interesting question : "Ethanol does not occur naturally in the body; so, why did Nature provide us with alcohol dehydrogenase unless she meant us to drink?" A diligent search through ...

PURPOSE To identify differentially expressed genes in keratoconus (KC) corneal fibroblasts. METHODS Stromal keratocytes (having a fibroblast morphology) from KC keratoplasty specimens and eye bank donor corneas were isolated and expanded using a serum containing medium. RNA was isolated from three KC fibroblast cultures and five eye bank donor cornea fibroblast cultures. The targets from the ...

Commercially available crystalline yeast alcohol dehydrogenase contained protein kinase activity. Casein and phosvitin were readily phosphorylated, but whole calf thymus histone was not. The protein kinase activity was inhibited by KCl, was not stimulated by cyclic AMP and could be separated from the alcohol dehydrogenase activity by sucrose density centrifugation.

In Nature, protons (H(+)) can mediate metabolic process through enzymatic reactions. Examples include glucose oxidation with glucose dehydrogenase to regulate blood glucose level, alcohol dissolution into carboxylic acid through alcohol dehydrogenase, and voltage-regulated H(+) channels activating bioluminescence in firefly and jellyfish. Artificial devices that control H(+) currents and H(+) c...

A hepatic microsomal ethanol-oxidizing system is described both in men and rats. It is distinguished from alcohol dehydrogenase by its subcellular localization (cytosol for alcohol dehydrogenase, microsomes for this system), its pH optimum (physiological pH versus pH 10 to 11 for alcohol dehydrogenase), and its cofactor requirements (NADPH versus NAD+ for alcohol dehydrogenase). It also require...

We have identified an alcohol dehydrogenase activity in Pseudomonas putida strains carrying the CAM-OCT degradative plasmid that were grown on octane. The activity is nicotinamide adenine dinucleotide independent, sediments at 48,000 x g, and shows 20-fold greater activity with octanol rather than butanol as substrate. The enzyme is inducible by unoxidized alkane and is present only in strains ...