Molecular Heterosis for Heat-Sensitive Enzyme Alleles
- 1 May 1974
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (5), 1808-1810
- https://doi.org/10.1073/pnas.71.5.1808
Abstract
Heat denaturation studies were carried out and revealed hidden genic variants with the same net charge at the Octanol dehydrogenase-1 locus in Drosophila pseudoobscura. Studies of several genetic crosses between strains with different heat-sensitivity alleles showed that the F1 retained more in vitro enzyme activity after being heat-treated for a specified amount of time at a given temperature than the heat-resistant parent. We call this phenomenon “heterosis for heat-stability of enzyme activity” and discuss its possible molecular mechanism, its relation to maintenance of genetic variation in natural populations, and its bearing on the “classical” and “balance” hypotheses.Keywords
This publication has 3 references indexed in Scilit:
- Still More Genetic Variability in Natural PopulationsProceedings of the National Academy of Sciences, 1973
- Electrophoretic Variation in EnzymesScience, 1965