Two isoenzymes of alcohol dehydrogenase have been purified from human stomach and characterized with regard to electrophoretic mobility and kinetic properties with ethanol, hexanol, and acetaldehyde. Both undergo a time-dependent formation of multiple electrophoretic bands; the total amount of alcohol dehydrogenase activity in an average human stomach is only about 0.2% of that of the liver.
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Hempel et al. (1979) studied this question.