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Gene Expression in Drosophila: Post-translational Modification of Aldehyde Oxidase and Xanthine Dehydrogenase

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Journal Mol Gen Genet
Date 1979 Apr 17
PMID 286873
Citations 8
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Abstract

Maroon-like homozygotes are completely deficient for xanthine dehydrogenase (XDH) and aldehyde oxidase (AO), however, ma-l is not a structural locus for either enzyme. Quantitative immunoelectrophoresis of ma-l and wild type extracts suggests that the ma-l function must be post-translational. To determine whether the ma-l function involves some direct physical changes in XDH and/or AO the enzymes were characterized with respect to temperature sensitivity and behavior in gel sieving electrophoresis. Since the XDH and AO from complementary ma-l heterozygotes is more thermolabile and different in shape from wild type XDH and AO, we conclude that ma-l is involved in a post-translational modification of these enzymes.

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References
1.
BUNN H, GABBAY K, Gallop P . The glycosylation of hemoglobin: relevance to diabetes mellitus. Science. 1978; 200(4337):21-7. DOI: 10.1126/science.635569. View

2.
Dizik M, Elliott R . A second gene affecting the sialylation of lysosomal alpha-mannosidase in mouse liver. Biochem Genet. 1978; 16(3-4):247-60. DOI: 10.1007/BF00484082. View

3.
Gelbart W, McCarron M, Chovnick A . Extension of the limits of the XDH structural element in Drosophila melanogaster. Genetics. 1976; 84(2):211-32. PMC: 1213573. DOI: 10.1093/genetics/84.2.211. View

4.
Dickinson W . The genetics of aldehyde oxidase in Drosophila melanogaster. Genetics. 1970; 66(3):487-96. PMC: 1212509. DOI: 10.1093/genetics/66.3.487. View

5.
Glassman E, PINKERTON W . Complementation at the maroon-like eye-color locus of Drosophila melanogaster. Science. 1960; 131(3416):1810-1. DOI: 10.1126/science.131.3416.1810. View