1977
DOI: 10.1111/j.1432-1033.1977.tb11613.x
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The Genetic Control of Molybdoflavoproteins in Aspergillus nidulans. A Xanthine Dehydrogenase I Half-Molecule in cnx- Mutant Strains of Aspergillus nidulans

Abstract: The cnx− group of mutants of Aspergillus nidulans lacks xanthine dehydrogenase (xanthine: NAD+ oxidoreductase, EC 1.2.1.37) and nitrate reductase (EC 1.6.6.3) activities and are thought to be defective in the synthesis of a molybdenum‐containing cofactor, ‘cnx’, common to xanthine dehydrogenase and nitrate reductase [Pateman, J. A., Rever, B. M., Cove, D. J. and Roberts, D. B. (1964) Nature (Lond.) 201, 58–60]. The cnx cofactor has a role in maintaining the aggregated multimeric structure of nitrate reductase … Show more

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Cited by 19 publications
(15 citation statements)
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“…Precipitin bands formed as lines of identity with active xanthine dehydrogenase present in liver tissue from control individuals and appeared to be equal in intensity. Bands were easily observable without staining but were intensified for photographic purposes by using an activity stain that requires functional flavin and Fe/S centers but is independent of the molybdenum cofactor (24 thesized in livers of tungsten-treated rats has also resisted all reconstitution attempts (unpublished observations). Assays of Molybdenum Cofactor.…”
Section: Resultsmentioning
confidence: 99%
“…Precipitin bands formed as lines of identity with active xanthine dehydrogenase present in liver tissue from control individuals and appeared to be equal in intensity. Bands were easily observable without staining but were intensified for photographic purposes by using an activity stain that requires functional flavin and Fe/S centers but is independent of the molybdenum cofactor (24 thesized in livers of tungsten-treated rats has also resisted all reconstitution attempts (unpublished observations). Assays of Molybdenum Cofactor.…”
Section: Resultsmentioning
confidence: 99%
“…The mutant strains showed a band, staining with all substrates and with identical mobility to the wild-type enzyme run in parallel and stained with each of the substrates. Crossed immunoelectrophoresis with a reference line under nonsieving conditions [26] showed complete antigenic identity between the mutant and wild-type enzymes and identical electrophoretic mobilities at both pH 6.5 ( Fig. 3) and 8.6.…”
Section: Physical Properties Of the Mutant Enzymementioning
confidence: 88%
“…For each determination, serial dilutions of the wild type induced with 2-thiouric acid and grown in parallel with the mutant were run as standards. After immunoelectrophoresis the plates were stained for NADH dehydrogenase activity as described previously [26]. The amount of cross-reacting material contained in the mutant was expressed relative to the wild type induced with 2-thiouric acid.…”
Section: Preparation Of Antibodiesmentioning
confidence: 99%
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