๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Variation in the biochemical properties of theDrosophilaalcohol dehydrogenase allozymes

โœ Scribed by Geoffrey K. Chambers; Ann V. Wilks; John B. Gibson

Book ID
104787557
Publisher
Springer
Year
1984
Tongue
English
Weight
822 KB
Volume
22
Category
Article
ISSN
0006-2928

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โœฆ Synopsis

Thirteen Drosophila Adh variants have been characterized with respect to gene expression, substrate preference, thermostability, and specific activity. The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.

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Polymorphism at the ฮฑ-glycerophosphate d
Polymorphism at the ฮฑ-glycerophosphate dehydrogenase locus inDrosophila melanogaster. I. Properties of adult allozymes
โœ Stephen Miller; Robert W. Pearcy; Edward Berger ๐Ÿ“‚ Article ๐Ÿ“… 1975 ๐Ÿ› Springer ๐ŸŒ English โš– 602 KB

A biochemical comparison was made between ~-glycerophosphate dehydrogenase allozymes from Drosophila melanogaster. Enzymes extracted from the three major genotypes were indistinguishable in terms of their pH optima and thermal stabilities. Distinctive differences were observed for three parameters;