Relative electrophoretic mobility (REM) of alcohol dehydrogenases from equine hepatocyte cytoplasm was low probably due to the presence of a loop which consisted of 21 amino acid residues in the surface layer of the enzyme subunits. The REM of multiple molecular forms of alcohol dehydrogenases from yeast cell cytoplasm was higher as consistent with the absence of this loop in the surface layer of the enzyme subunits. Possible role of amino acid residues comprising the loop, in the formation of total charge and their effect on REM values of enzymes from the alcohol/polyol dehydrogenase family are discussed.
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