Preliminary characterization and physical properties of pyridoxal oxidase activity from Drosophila melanogaster

1980 ◽  
Vol 180 (2) ◽  
pp. 455-462 ◽  
Author(s):  
E. W. Hanly
1978 ◽  
Vol 20 (4) ◽  
pp. 489-497 ◽  
Author(s):  
Eva M. Meidinger ◽  
John H. Williamson

Four different genes are known to affect aldehyde oxidase activity (AO) in Drosophila melanogaster. Mutants at each of these loci eliminate AO activity and simultaneously eliminate detectable AO-crossing reacting material (AO-CRM) even though only one is the structural gene for AO (Aldoxn). The other three genes (cin1, lxd and mal) coordinately "control" the levels of activity of AO and two related enzymes, xanthine dehydrogenase (XDH) and pyridoxal oxidase (PO). Contrary to their effects on AO-CRM, neither of these three mutants eliminate XDH-CRM. A model of interaction of these enzymes and genes controlling their activities is discussed.


Genetics ◽  
1977 ◽  
Vol 85 (3) ◽  
pp. 489-496
Author(s):  
Richard L Roehrdanz ◽  
James M Kitchens ◽  
John C Lucchesi

ABSTRACT Aldehyde oxidase activity has been measured in flies with the structural gene for this enzyme translocated to the X chromosome. These measurements are presented as experimental evidence that, in Drosophila melanogaster, an autosomal gene relocated to the X chromosome is not dosage compensated.


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