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THE CHARACTERIZATION OF 
-GLYCEROPHOSPHATE DEHYDROGENASE
MUTANTS IN DROSOPHILA MELANOGASTER
Michael A. Kotarski 1, Sally Pickert 1, Deborah A. Leonard 1, Gregory J. LaRosa 1, and Ross J. MacIntyre 1
1 Section of Genetics and Development, Cornell University, Ithaca,
New York 14853
Thirty mutants of 
-glycerophosphate dehydrogenase (GPDH,
EC 1.1.1.8) from Drosophila melanogaster were produced with the chemical
mutagen ethyl methanesulfonate (EMS). These mutants and nine others previously
obtained have been characterized with respect to level of enzymatic activity,
viability, flight ability, and presence of cross-reacting material (CRM).
The presence of GPDH mRNA in several of the mutants has been tested
by in vitro translation. There are strong correlations between the
level of enzyme activity, viability and flight ability. Thirteen of the mutants
are CRM- by solution immunoprecipitation experiments, but
of these, only three are CRM- by a more sensitive 125
I-protein A-based radioimmune gel assay. The viability of the three
CRM- mutants suggests that the absence of GPDH protein
is not a lethal condition. The immunoprecipitated protein of the low activity
mutant, GpdhnGL3, has a smaller apparent molecular
weight on polyacrylamide-SDS gels than does the protein from wild type. Criteria
for the identification of nonsense mutations in Drosophila are discussed.
Accepted on June 9, 1983
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