ALCOHOL DEHYDROGENASE-NEGATIVE MUTANTS IN DROSOPHILA: DEFECTS AT THE STRUCTURAL LOCUS?
Author(s) -
Marcia Schwartz,
William Sofer
Publication year - 1976
Publication title -
genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.792
H-Index - 246
eISSN - 1943-2631
pISSN - 0016-6731
DOI - 10.1093/genetics/83.1.125
Subject(s) - alcohol dehydrogenase , complementation , biology , mutant , structural gene , ethyl methanesulfonate , alcohol oxidoreductase , locus (genetics) , genetics , gene , enzyme , sodium dodecyl sulfate , biochemistry , gel electrophoresis , microbiology and biotechnology , nad+ kinase
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 complementation, sodium dodecyl sulfate electrophoresis and antibody precipitation. Eleven of the sixteen negative strains showed evidence of inactive ADH protein and are presumably mutations in the structural element. These results are discussed in light of some recent models of gene organization in higher organisms.
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