Abstract
A maximum of 22 bands comprising four esterase subgroups—acetylesterase, carboxylesterase, cholinesterase, and acetylcholinesterase—were detected following electrophoresis of lesser snow goose sera on polyacrylamide gels. A minimum of seven structural genes was surmised to be involved in the biosynthesis of these enzymes following physiochemical characterizations. The genetic variability of these loci was calculated to be 1.25% average heterozygosity, while 14.3% of the loci were polymorphic. These estimates of genetic variability were substantially lower than those reported for other vertebrate species. The low degree of genetic variability found in snow goose serum esterases coupled with the extensive protein multiplicity observed may possibly reflect an adaptive strategy based on “biochemical plasticity” rather than genic heterozygosity for this species. The nature of evolutionary forces acting upon multiple enzyme systems such as esterases is discussed. The concept of “conditional neutrality” is introduced and defined within this context.
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This research was carried out under grants from the National Research Council of Canada and the Canadian Wildlife Service to F. Cooke. J. Grossfield was supported by grants from the National Institutes of Health, GM 21630 and FRAP 10576.
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Bargiello, T.A., Grossfield, J., Steele, R.W. et al. Isoenzyme status and genetic variability of serum esterases in the lesser snow goose, Anser caerulescens caerulescens . Biochem Genet 15, 741–763 (1977). https://doi.org/10.1007/BF00484101
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DOI: https://doi.org/10.1007/BF00484101