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Variation between electrophoretically identical alleles at the alcohol dehydrogenase locus inDrosophila melanogaster

✍ Scribed by G. E. W. Thörig; A. A. Schoone; W. Scharloo


Publisher
Springer
Year
1975
Tongue
English
Weight
514 KB
Volume
13
Category
Article
ISSN
0006-2928

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✦ Synopsis


A new variant of alcohol dehydrogenase (ADH 7lk) was found in a laboratory stock of Drosophila melanogaster. ADH in this stock had the same electrophoretic mobility as the F variant both on acrylamide and on agar. Activity levels were similar to the levels in F flies at temperature between 15 and 25 C. But while ADH F enzyme is inactivated rapidly at 40 C, ADH 7lk is still active. Also, ADH S is not inactivated at this temperature, but has a far lower activity per fly than ADH 7lk. Genetic analysis showed that the new variant is an allele of the Adh locus.


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We have examined the kinetic properties of enzymes produced by the electrophoretically fast (F) and slow (S) alleles at the alcohol dehydrogenase locus in a polymorphic laboratory population of Drosophila melanogaster. The product of the F allele has approximately twice the specific activity of the