Properties of alcohol dehydrogenase isozymes in a strain of Drosophila melanogaster homozygous for the Adh-slow allele View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1974-02

AUTHORS

Thomas H. Day, L. Needham

ABSTRACT

Two isozymes of alcohol dehydrogenase from Drosophila melanogaster homozygous for the Adh-slow allele have been separated by isoelectric focusing. The isozymes differ in their temperature optima, temperature stabilities, specific activities, and at least one of their Michaelis constants. They are immunologically identical. Evidence is presented that NAD may partially convert one isozyme into another. The possible nature of these isozymic differences is discussed. More... »

PAGES

167-175

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00485772

DOI

http://dx.doi.org/10.1007/bf00485772

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005145423

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4363212


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