Electronic properties of the metallic perovskite LaNiO3: Correlated behavior of 3d electrons.
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Journal Article↗
Biomedical subjects
M McElfresh
Publications and source records attributed to M McElfresh.
Alcohol-oxidizing enzymes in 13 Drosophila species.
Starch and polyacrylamide gel electrophoresis were used to ascertain the substrate specificities of alcohol-oxidizing enzymes in 13 Drosophila species. The substrates used were a variety of long- and short-chain aliphatic alcohols, one aromatic alcohol, and benzaldehyde. Only one enzyme (product of a single-gene locus) showed significant NAD+-dependent alcohol dehydrogenase activity with short-chain aliphatic alcohols. The 13 species, belonging to four different Drosophila groups, all showed a similar complement of alcohol-oxidizing enzymes, although differences in electrophoretic mobility and in levels of activity existed from species to species. These findings are relevant to the adaptation of Drosophila to alcohol environments.
Alcohol Oxidoreductases↗