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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 151 (1968), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Development genes and evolution 188 (1980), S. 91-99 
    ISSN: 1432-041X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Black cells (Bc, 2-80.6±) mutant larvae ofDrosophila melanogaster have pigmented cells in the hemolymph and lymph glands. In this report we present evidence that these melanized cells are a mutant form of the crystal cells, a type of larval hemocyte with characteristic paracrystalline inclusions.Bc larvae lack crystal cells. Furthermore, the distribution pattern of black cells inBc larvae parallels that of experimentally-blackened crystal cells in normal larvae (phenocopy).InBc/Bc zygotes black cells appear during mid embryonic development but inBc +/Bc zygotes pigmented cells are not found until late in the first larval instar.Crystal cells are present in the heterozygous larvae until this time, and paracrystalline inclusions can be seen in some of the cells undergoing melanization in these larvae.The rate of phenol oxidase activity inBc +/Bc larval cell-free extracts is less than half that ofBc +/Bc +extracts whereas enzyme activity is undetectable inBc/Bc larvae. We propose that theBc +gene product is required for maintaining the integrity of the paracrystalline inclusions; inBc/Bc larvae either the product is absent or nonfunctional so an effective contact between substrate and enzyme results in melanization of the cells.Phenol oxidase itself is either destroyed or consumed in the melanization process accounting for the absence of enzyme activity inBc/Bc larvae. These studies confirm that the crystal cells store phenolic substrates and are the source of the hemolymph phenol oxidase activity in the larva ofD. melanogaster.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 11 (1974), S. 359-365 
    ISSN: 1573-4927
    Keywords: lozenge ; phenol oxidase ; Drosophila melanogaster ; tyrosinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have found that the phenol oxidase activity in 50-hr Drosophila melanogaster pupae is much greater than that of adult flies. The mutants lz and lz g have all of the phenol oxidase components present in wild type, whereas the mutant tyr-1 has all of the wild-type components but the activity of each component is greatly reduced in comparison with wild-type activity. The newly discovered lozenge allele, lz rfg, lacks all phenol oxidase activity.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 13 (1975), S. 353-356 
    ISSN: 1573-4927
    Keywords: suppression ; Drosophila ; phenol oxidase ; speck
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A marked decrease in the amount of the A2 component of phenol oxidase occurs in the speck locus of Drosophila melanogaster. The amount of A2 in speck is restored to a normal amount in the presence of the suppressor mutant, su(s) 2.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4927
    Keywords: sepiapterin synthase ; variegation ; purple ; Drosophila melanogaster ; pteridine eye pigments ; drosopterin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A variegated position effect on the autonomous gene, purple, has been studied enzymologically in Drosophila melanogaster. Sepiapterin synthase, the enzyme system associated with pr +, was examined for activity in different developmental stages of the fly. The results indicate that T(Y:2) pr c5, cn/prc4 cn flies (flies in which pr + has been translocated and which exhibit variegation) have a reduced amount of enzyme activity as compared with both Oregon-R and pr 1 flies. This reduction in activity was not found in larval stages, which suggests that the inactivation process probably occurs in late larval or early pupal stages. The phenotype of the variegated adult has white eyes with red-colored spots and patches where drosopterins occur. The phenotype of the fly carrying the translocation is modified by the presence of additional Y chromosomes. This extends the observation from other systems that extra heterochromatin acts to suppress the variegated position effect. The advantages of studying the variegation by measuring enzyme activity, as well as the phenotypic expression, are several; for example, the developmental time at which variegation occurs may be estimated even though drosopterin synthesis is not occurring.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-4927
    Keywords: Drosophila ; vermilion ; tryptophan oxygenase ; suppression ; epigenetic suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The suppressor gene,su(s)2, inDrosophila melanogaster restores the production of red and brown eye pigments for some purple and vermilion mutant alleles, respectively. We showed previously that the product of thesu(s)+ allele caused inhibition of the sepiapterin synthase A produced by the purple mutant but did not affect the wild-type enzyme. Suppression was accomplished by removingsu(s)+ from the genome. We now report that the tryptophan oxygenase, produced by suppressible vermilion alleles, is also inhibited by extracts fromsu(s)+ flies. The inhibition of the vermilion enzyme can be reduced or eliminated, respectively, by prior storage of the extract at 4 or −20°C or by boiling, whereas the wild-type enzyme is not affected by extracts ofsu(s)+ flies. Also, when the suppressible vermilion strain is raised on certain diets, brown eye pigment production occurs. This epigenetic suppression was reduced by the presence of an extra copy ofsu(s)+ in the genome. These data support a posttranslational mechanism for regulation of enzyme activity in which the activity of the mutant enzyme is reduced by the product of thesu(s)+ allele. How thesu(s)+ gene product can distinguish between the normal and the mutant forms of these two enzymes is discussed, along with other mechanisms for suppression that are currently under investigation.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 93 (1962), S. 371-377 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two loci,ma-l + andry +, necessary for xanthine dehydrogenase activity inDrosophila melanogaster have been studied for dosage effects utilizing deficiencies and duplications induced for this purpose. Comparisons of one, two and three doses ofma-l + in the female or one and two doses in the male indicate that there is no increase in specific enzyme activity with dose. On the other hand, comparisons of one, two and three doses ofry + in the male and female reveal an increase in enzyme activity that is roughly proportional to dose. Since dosage ofry + is limiting, whereas that ofma-l + is not, the final concentration of xanthine dehydrogenase is shown to depend on the number of doses ofry +. The implications of these findings with respect to the hypothesis of dosage compensation and to the mechanism of control of enzyme and protein concentration are discussed.
    Type of Medium: Electronic Resource
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