ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Biochemical genetics 24 (1986), S. 683-699 
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; aldox-2 ; molybdoenzymes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract The aldox-2 locus in Drosophila melanogaster has been shown to affect differentially three molybdoenzymes, aldehyde oxidase, pyridoxal oxidase, and xanthine dehydrogenase. These effects are most obvious at times surrounding the pupal-adult boundary, when the normal organism accumulates large amounts of these enzymes in their active form. This locus has been more precisely mapped genetically to 2–82.9±2.1, with complete concordance between the effects of all recombinant chromosomes on all three enzymes. The cytogenetic location has also been determined to be between 52E and 54E8, with the likelihood that it lies within the region 54B1-54E8. The aldox-2 mutant allele has no visible phenotype and is completely recessive for enzyme effects at all stages tested. Segmental duplication of this region, including the aldox-2 + allele, has no apparent effect on the visible phenotype or the enzymatic activity. The mutant aldox-2 allele has no effect on the developmental expression of two unrelated enzymes, 6-phosphogluconate dehydrogenase and NADP+-dependent isocitrate dehydrogenase. The effects of this locus on aldehyde oxidase, xanthine dehydrogenase, and pyridoxal oxidase suggest that this locus may code for a product involved in the synthesis of the molybdenum cofactor common to these enzymes.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Biochemical genetics 24 (1986), S. 291-308 
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; aldehyde oxidase ; gene dosage ; Aldox
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Aldox “null” alleles which were isolated from natural populations in Great Britain and North Carolina were analyzed for complementation. No complementation was observed between any combinations of “null” alleles for aldehyde oxidase (AO) specific activity in late third-instar larvae and newly emerged adults. AO immunologically cross-reacting material (AO-CRM) was quantitated in all homozygous stocks at both developmental stages as well as all allelic combinations in newly emerged adults. When the adult organism contains only Aldox n alleles, the polypeptides are not immunologically recognizable or may be rapidly degraded. Larvae and adults have different abilities to degrade mutationally altered enzymatically inactive AO polypeptide or synthesize them differentially. This is indicated by easily measurable AO-CRM levels in late third-instar larvae of Aldox n homozygotes, while newly emerged adult Aldox n homozygotes have very little, if any, AO-CRM. Newly emerged adult heterozygotes of Aldox n /Aldox + do have increased AO-CRM, indicating that the Aldox n alleles can code for a polypeptide which can be “rescued” if Aldox + gene product is present. Heterozygotes containing an Aldox + allele with a deficiency for the Aldox region produce 74.2% of the AO-CRM found in Aldox + homozygotes. This may indicate the presence of trans-acting factors which serve to activate gene expression in a system in which each gene copy is not maximally expressed.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; mex ; NADP+ ; NADPH ; malic enzyme
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract The isolation and characterization of mutant alleles in a regulatory gene affecting NADP+-dependent enzymes are described. The locus,mex, is at position 26.5 ± 0.74 on the X chromosome ofDrosophila melanogaster. The newly isolated mutant allele,mex 1, is recessive to either themex allele found in Oregon-R wild-type individuals or that found in thecm v parental stock in which the new mutants were induced. Themex 1 mutant allele is associated with statistically significant decreases in malic enzyme (ME) specific activity and ME specific immunologically cross-reacting material (ME-CRM) in newly emerged adult males. During this same developmental stage in males, the NADP+-dependent isocitrate dehydrogenase specific activity increases to statistically significant levels. Females of themex 1 mutant strain show statistically significant elevated levels of the pentose phosphate shunt enzymes, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Isoelectric focusing and thermolability comparisons of the active ME from mutant and control organisms indicate that the enzyme is the same. Developmental profiles ofmex 1 and control strains indicate that this mutant allele differentially modulates the levels of ME enzymatic activity and ME-CRM during development.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Biochemical genetics 27 (1989), S. 99-118 
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; aldox-2 ; molybdoenzymes ; sulfite oxidase ; molybdenum ; tungsten
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Mutation at thealdox-2 locus inDrosophila melanogaster affects the specific activities of four molybdoenzymes differentially during development. Sulfite oxidase activity is normal during late larval and pupal stages but is reduced during early adult stages inaldox-2 organisms. There was complete concordance among the effects ofaldox-2 on sulfite oxidase, aldehyde oxidase, xanthine dehydrogenase, and pyridoxal oxidase, when 38 stocks were analyzed which were derived from single recombination events betweenc andpx, markers which flankaldox-2. Several different biochemical analyses indicate that the active molybdoenzymes present in thealdox-2 strain are normal with respect to size, shape,pH-activity profile,K m , and molecular weight. Significant differences were found between thealdox-2 strain and the OR control strain in their responses to dietary Na2MoO4 and Na2WO4. The mutant strain is much more resistant to the effects of dietary Na2WO4 and much more responsive to the administration of Na2MoO4 than the OR control strain when these effects are quantitated by measurements of molybdoenzyme specific activities. This evidence suggests that thealdox-2 + gene product has a molybdenum binding site which can also bind tungsten and that this site is altered in the mutant strain. The hypothesis presented explains the observed effects of thealdox-2 mutation and relates them to the other mutations reported in this gene-enzyme system.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    Digitale Medien
    Digitale Medien
    Springer
    Biochemical genetics 31 (1993), S. 375-391 
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; sulfite oxidase ; molybdenum ; MoCo
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract The relationship between sulfite oxidase (SO) and sulfite sensitivity inDrosophila melanogaster is addressed. Significant improvements to the SO assay have provided an investigative tool which can be applied to further studies of this molybdoenzyme. Using the second-instar larval stage ofD. melanogaster, we have shown a direct relationship between measured levels of sulfite oxidase activity and the organism's ability to withstand a sulfite challenge. Implementation of a sulfite-testing procedure confirmed the documented instability of sulfite in solution and may explain some of the conflicting results reported in the SO literature. Results of the tungstate-addition experiments confirm thatDrosophila SO is a molybdoenzyme and its activity was shown to be governed by three of the four loci known to affect more than one molybdoenzyme. The ability ofD. melanogaster to withstand the application of exogenous sulfites is shown to be dependent on sulfite oxidase activity.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 6
    Digitale Medien
    Digitale Medien
    Springer
    Biochemical genetics 31 (1993), S. 375-391 
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; sulfite oxidase ; molybdenum ; MoCo
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract The relationship between sulfite oxidase (SO) and sulfite sensitivity inDrosophila melanogaster is addressed. Significant improvements to the SO assay have provided an investigative tool which can be applied to further studies of this molybdoenzyme. Using the second-instar larval stage ofD. melanogaster, we have shown a direct relationship between measured levels of sulfite oxidase activity and the organism's ability to withstand a sulfite challenge. Implementation of a sulfite-testing procedure confirmed the documented instability of sulfite in solution and may explain some of the conflicting results reported in the SO literature. Results of the tungstate-addition experiments confirm thatDrosophila SO is a molybdoenzyme and its activity was shown to be governed by three of the four loci known to affect more than one molybdoenzyme. The ability ofD. melanogaster to withstand the application of exogenous sulfites is shown to be dependent on sulfite oxidase activity.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 7
    ISSN: 1573-4927
    Schlagwort(e): Drosophila ; mex ; NADP+ ; NADPH ; malic enzyme
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract The isolation and characterization of mutant alleles in a regulatory gene affecting NADP+-dependent enzymes are described. The locus,mex, is at position 26.5 ± 0.74 on the X chromosome ofDrosophila melanogaster. The newly isolated mutant allele,mex 1, is recessive to either themex allele found in Oregon-R wild-type individuals or that found in thecm v parental stock in which the new mutants were induced. Themex 1 mutant allele is associated with statistically significant decreases in malic enzyme (ME) specific activity and ME specific immunologically cross-reacting material (ME-CRM) in newly emerged adult males. During this same developmental stage in males, the NADP+-dependent isocitrate dehydrogenase specific activity increases to statistically significant levels. Females of themex 1 mutant strain show statistically significant elevated levels of the pentose phosphate shunt enzymes, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Isoelectric focusing and thermolability comparisons of the active ME from mutant and control organisms indicate that the enzyme is the same. Developmental profiles ofmex 1 and control strains indicate that this mutant allele differentially modulates the levels of ME enzymatic activity and ME-CRM during development.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 8
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 99 (1987), S. 1172-1173 
    ISSN: 0044-8249
    Schlagwort(e): Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 9
    ISSN: 0044-8249
    Schlagwort(e): Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 10
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...