The determination of aldehyde oxidase activity patterns in the wing discs of Drosophila melanogaster

1986 ◽  
Vol 195 (5) ◽  
pp. 338-343 ◽  
Author(s):  
Edward McCrady ◽  
Th. E. Sprey
Keyword(s):  
Drosophila Melanogaster ◽  
Oxidase Activity ◽  
Activity Patterns ◽  
Aldehyde Oxidase ◽  
Wing Discs

scholarly journals A Highly Sensitive RP-HPLC-Fluorescence Method to Study Aldehyde Oxidase Activity

2011 ◽  
Vol 94 (2) ◽  
pp. 550-554 ◽  
Author(s):  
Mohammad-Reza Rashidi ◽  
Kaveh Amini ◽  
Mohammad-Yaser Khani ◽  
Akram Faridi ◽  
Jalal Hanaee ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Mobile Phase ◽  
Heterocyclic Compounds ◽  
Aldehyde Oxidase ◽  
Rapid Analysis ◽  
Fluorescence Method ◽  
Rp Hplc ◽  
Highly Sensitive ◽  
Extensive Range

Abstract Aldehyde oxidase is a widely distributed enzyme that is involved in the metabolism of an extensive range of aldehydes and N-heterocyclic compounds with physiological, pharmacological, and toxicological relevance. In the present study, a highly sensitive RP-HPLC-fluorescence method based on the oxidation of phenanthridine to phenanthridinone has been developed and validated to assay aldehyde oxidase activity in biological samples. Determination of phenanthridinone was achieved on a C18 column using 10 mmol/L phosphate buffer (pH 5.0) containing 0.1 mmol/L EDTAacetonitrile (40 60, v/v) as the mobile phase. The fluorescence intensity of phenanthridinone was measured at 364 nm with excitation at 236 nm. The proposed method was precise, accurate, specific and rapid (analysis time, approximately 8 min) with a mean RSD of 2.54. Peak responses were linear from 0.5 to 100 nmol/L, with an LOD of 0.125 nmol/L. The applicability of the method was demonstrated by measurement of aldehyde oxidase activity in rat liver, kidney, ovary, and heart fractions.

scholarly journals LACK OF DOSAGE COMPENSATION FOR AN AUTOSOMAL GENE RELOCATED TO THE X CHROMOSOME IN DROSOPHILA MELANOGASTER

Genetics ◽  
1977 ◽  
Vol 85 (3) ◽  
pp. 489-496
Author(s):  
Richard L Roehrdanz ◽  
James M Kitchens ◽  
John C Lucchesi
Keyword(s):  
Drosophila Melanogaster ◽  
Experimental Evidence ◽  
Structural Gene ◽  
X Chromosome ◽  
Dosage Compensation ◽  
Oxidase Activity ◽  
Aldehyde Oxidase ◽  
Autosomal Gene

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.

THE EFFECTS OF LAO ON ALDEHYDE OXIDASE ACTIVITY AND CROSS-REACTING-MATERIAL IN DROSOPHILA MELANOGASTER

1978 ◽  
Vol 20 (4) ◽  
pp. 545-553 ◽  
Author(s):  
John H. Williamson ◽  
Michael M. Bentley ◽  
Melvin J. Oliver ◽  
Billy W. Geer
Keyword(s):  
Drosophila Melanogaster ◽  
Oxidase Activity ◽  
Mutant Allele ◽  
Aldehyde Oxidase ◽  
Wild Type ◽  
Heat Labile ◽  
Major Form ◽  
Normal Enzyme ◽  
Mutant Stock

In Drosophila melanogaster aldehyde oxidase occurs in at least two forms that can be separated electrophoretically. The mutant allele lao (low aldehyde oxidase activity) causes a deficiency of the major form of this enzyme. Immunoelectrophoretic analyses suggest that lao homozygotes produce aldehyde oxidase cross-reacting-material in nearly wild-type levels. Although aldehyde oxidase from the mutant stock is heat labile, properties such as Km and pH optima are not different from the normal enzyme.

GENETIC CONTROL OF ALDEHYDE OXIDASE ACTIVITY AND CROSS-REACTING-MATERIAL IN DROSOPHILA MELANOGASTER

1978 ◽  
Vol 20 (4) ◽  
pp. 489-497 ◽  
Author(s):  
Eva M. Meidinger ◽  
John H. Williamson
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Control ◽  
Structural Gene ◽  
Oxidase Activity ◽  
Aldehyde Oxidase ◽  
Xanthine Dehydrogenase ◽  
The Other ◽  
Pyridoxal Oxidase

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.

THE DEVELOPMENTAL ANALYSIS OF ALDEHYDE OXIDASE ACTIVITY IN CIN ALLELIC HETEROZYGOTES OF DROSOPHILA MELANOGASTER

1982 ◽  
Vol 24 (1) ◽  
pp. 1-9 ◽  
Author(s):  
M. M. Bentley ◽  
J. H. Williamson
Keyword(s):  
Drosophila Melanogaster ◽  
Oxidase Activity ◽  
Developmental Stages ◽  
Aldehyde Oxidase ◽  
Activity Levels ◽  
Developmental Analysis

Aldehyde oxidase (AO) activity has been determined at 11 stages during the development of selected cin allelic homo-, hemi- and heterozygotes in Drosophila melanogaster. The AO activity levels found during development were completely consistent with the levels previously reported for adults, less than 24 h of age (Bentley and Williamson, 1979b). All of the cin homo- and hemizygotes tested exhibited no significant levels of AO activity at any of the 11 stages during development. All cin allelic heterozygotes, which were defined as complementing in adults, less than 24 h of age, displayed similar levels of complementation at all stages tested. Conversely, all cin allelic heterozygotes which were defined as noncomplementing in adults, less than 24 h of age, were found to lack measurable AO activity at all developmental stages tested.

A rapid and sensitive fluorometric method for determination of aldehyde oxidase activity

2018 ◽  
Vol 341 ◽  
pp. 30-37 ◽  
Author(s):  
Nancy Apenova ◽  
Hui Peng ◽  
Markus Hecker ◽  
Markus Brinkmann
Keyword(s):  
Oxidase Activity ◽  
Aldehyde Oxidase ◽  
Fluorometric Method
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