Diet-induced alterations in distribution of multiple forms of alcohol dehydrogenase in Drosophila View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1976-09

AUTHORS

MARCIA SCHWARTZ, WILLIAM SOFER

ABSTRACT

IT is now well accepted that enzyme polymorphisms are widespread among organisms. Electrophoretic polymorphisms in particular have been extensively studied and discussed1. One enzyme, alcohol dehydrogenase (ADH) has received special attention because the relative proportions of two polymorphic forms (allozymes), AdhF and Adhs, in Drosophila, seem to vary with environmental temperature2,3. The situation with regard to Drosophila ADH, however, is complicated by the fact that even in flies homozygous for a given electrophoretic variant or allozyme, three forms of ADH activity are observed after electrophoresis4–6. They are distributed in such a way that (on agar gel electrophoresis) the one which migrates most cathodally (termed ADH5 in the AdhF strain) has the highest activity, but is the least stable to heat. The least cathodally migrating form (ADH1 in the AdhF strain) has the least activity and is the most heat stable, whereas the third form (ADH3 in the AdhF strain) is intermediate with respect to both activity and heat stability (Fig. 1a). These forms are termed isozymes, in order to contrast them with the allozymes described above. More... »

PAGES

129-131

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/263129a0

DOI

http://dx.doi.org/10.1038/263129a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051342864

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/184393


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