Abstract
Sixteen Adh-negative mutants (induced by ethyl methanesulfonate) were examined for the presence of inactive alcohol dehydrogenase (ADH) protein. Four techniques were utilized in an effort to detect this protein: hybrid enzyme formation, intra-cistronic complentation, sodium dodecyl sulfate electrophoresis and antibody precipitation. Eleven of the sixteen negative strains showed evidence of inactive ADH protein and are preseumably mutations in the strutural element. These results are discussed in light of some recent models of gene organization in higher organisms.