Biochemical characterization of the products of the Adh loci of Drosophila mojavensis

Abstract

The electrophoretic pattern of alcohol dehydrogenase (ADH) of Drosophilia mojavensis is composed of multiple bands. In previous studies from this laboratory we suggested on the basis of genetic evidence that multiple ADH bands were due to the presence of a gene duplication. In the studies presented here, this hypothesis is supported by data derived from comparing the protein biochemistry of each ADH. Three forms of D. mojavensis ADH have been isolated. These are the ADH-1 homodimer, the ADH-2 homodimer, and the ADH-1 ADH-2 interlocus heterodimer. Each of these isozymes has a native molecular weight of approximately 50,000. Each native molecule is composed of two subunits of identical size, 2..