Abstract
The level of hidden variation in populations of Drosophila melanogaster at the Gpdh + locus was determined by thermal stability studies of the protein. The results indicate a lack of variation using these methods both in and between the two common electrophoretic variants. It is suggested that α-GPDH is conserved in primary structure, which may be related to its critical role in flight muscle metabolism.
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This investigation was supported by NIH Research Grants No. GM-11546 and GM-23617. Paper No. 5262 of the Journal Series of the North Carolina Agricultural Experiment Station, Raleigh, North Carolina 27607.
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Bewley, G.C. Heat stability studies at the α-glycerophosphate dehydrogenase locus in populations of Drosophila melanogaster . Biochem Genet 16, 769–775 (1978). https://doi.org/10.1007/BF00484734
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DOI: https://doi.org/10.1007/BF00484734