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. 1978 Jan;75(1):395–399. doi: 10.1073/pnas.75.1.395

Structural flexibility of isozyme variants: genetic variants in Drosophila disguised by cofactor and subunit binding.

G B Johnson
PMCID: PMC411255  PMID: 203939

Abstract

Wild populations of Drosophila mojavensis exhibit considerable conformational variation in the NAD+-free form of alcohol dehydrogenase (alcohol:NAD+ oxidoreductase; EC 1.1.1.1). The variation appears genetic, as it does not occur within an inbred strain. The NAD+-bound form of alcohol dehydrogenase, present in the same individuals, does not exhibit the variation, suggesting that the binding of NAD+ acts to stabilize conformation. Such cofactor binding to enzymes may thus conceal considerable variation. A similar effect is suggested for binding of esterase subunits.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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