Abstract
Enzyme polymorphism was characterized among the proteins of 14 loci of Coliae meadii by replicate electrophoresis in polyacrylamide gels of differing pore size. The results reveal a large number of variants, with a very skewed frequency distribution. A large fraction of the variants cannot be differentiated by electrophoresis in 5–7% acrylamide gels. This gel sieving approach permits an estimate of the relative contributions of charge and of conformation to electrophoretic mobility. Many of the variant proteins do not differ in charge. Most variants exhibit different degrees of interaction with the gel and presumably differ in conformation.
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This work was supported by grants from Washington University, the American Philosophical Society, the National Institutes of Health, and the National Science Foundation. Analysis was developed and carried out while the author was a Carnegie Institution of Washington Fellow.
Carnegie Institution of Washington Department of Plant Biology Publication No. 569.
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Johnson, G.B. Characterization of electrophoretically cryptic variation in the alpine butterfly Colias meadii . Biochem Genet 15, 665–693 (1977). https://doi.org/10.1007/BF00484097
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DOI: https://doi.org/10.1007/BF00484097