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  • 1
    Electronic Resource
    Electronic Resource
    Molecular anisotropy of the early Drosophila embryo (1975)
    [s.l.] : Nature Publishing Group
    Nature 258 (1975), S. 157-159 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Kock and Heinig4 and Nuneman and Moser5 first approached the problem of unequally distributed molecules in insect eggs by microelectrophoresis and immunoelectro-phoresis of parts of the egg of Achaeta domestica. They found quantitative differences between the anterior and posterior halves of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/258157a0
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  • 2
    Electronic Resource
    Electronic Resource
    The X-linked α-chain gene of Drosophila LSP-1 does not show dosage compensation (1979)
    [s.l.] : Nature Publishing Group
    Nature 280 (1979), S. 691-692 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Table 1 Amounts of a-chain found in the haemolymph of Drosophila larvae a, and ? as % of total a/ 4"V* protein t Mean s.d. Mean s.d. Oregon R females 0.42 0.04 60 4.1 Oregon R males 0.21 0.02 55.5 4.2 Samarkand females 0.51 0.06 58.1 2.6 Samarkand males 0.23 0.05 52.4 3.6 W/FM7 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/280691a0
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  • 3
    Electronic Resource
    Electronic Resource
    Antigens of Developing Drosophila melanogaster (1971)
    [s.l.] : Nature Publishing Group
    Nature 233 (1971), S. 394-397 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The changes in the antigenic complements of extracts of soluble proteins of Drosophila have been followed through ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/233394a0
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  • 4
    Electronic Resource
    Electronic Resource
    Quantitative in situ hybridization reveals extent of sequence homology between related DNA sequences in Drosophila melanogaster (1981)
    Springer
    Chromosoma 83 (1981), S. 159-168 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Cloned DNA from the larval serum protein one (LSP-1) genes was hybridized to polytene chromosomes of D. melanogaster. The ratio of grains deposited over any two of the three LSP-1 genes with any one LSP-1 subunit probe was constant. Varying the gene dose of any one LSP-1 subunit relative to the others by up to six fold gave a linear relationship of grain ratios to gene ratios. We show that these constant ratios closely reflect the extent of sequence homology between the genes as determined by heteroduplex mapping (Smith et al., 1981) and thermal denaturation studies. The results obtained demonstrate that the LSP-1 subunit genes are present in equal copies in the genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00286786
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  • 5
    Electronic Resource
    Electronic Resource
    Drosophila hemolymph proteins: Purification, characterization, and genetic mapping of larval serum protein 2 in D. melanogaster (1978)
    Springer
    Biochemical genetics 16 (1978), S. 101-119 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; hemolymph proteins ; gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three of the major protein species present in the hemolymph of Drosophila melanogaster larvae just prior to pupation are absent from second instar larvae but accumulate rapidly during the third instar. This article describes the purification and characterization of one of these, larval serum protein (LSP) 2, using an immunological assay. It is a homohexamer of molecular weight about 450,000, with a polypeptide molecular weight of 78,000–83,000. Fast and slow electrophoretic variants of this protein map between the markers vin and gs, at 36–37 on chromosome 3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484387
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  • 6
    Electronic Resource
    Electronic Resource
    The LSP1-α gene is not dosage compensated in the Drosophila melanogaster species subgroup (1982)
    Springer
    Biochemical genetics 20 (1982), S. 287-296 
    Details
    ISSN: 1573-4927
    Keywords: larval serum protein ; dosage compensation ; Drosophila melanogaster subgroup species
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The X-linked α subunit of larval serum protein 1 (LSP1-α) is shown to lack dosage compensation in six members of the melanogaster species subgroup, viz., Drosophila melanogaster, D. simulans, D. mauritiana, D. erecta, D. yakuba, and D. teissieri, by quantitative filter hybridization and by electrophoretic and autoradiographic analyses of fat body proteins. These results support the hypothesis that there is little selection pressure on the LSP1-α gene to acquire dosage compensation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484425
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  • 7
    Electronic Resource
    Electronic Resource
    Quantitative analysis of the amount of larval serum protein-1 (LSP-1) synthesized by flies with different doses of the LSP-1 coding sequences (1984)
    Springer
    Biochemical genetics 22 (1984), S. 783-795 
    Details
    ISSN: 1573-4927
    Keywords: larval serum protein ; gene dosage ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Larval serum protein-1 (LSP-1) and LSP-2 are the major proteins of Drosophila larval serum. The amount of LSP-1 synthesized is strictly proportional to the number of LSP-1 genes present within the range 1–10. The normal number in female flies is 6. Flies with extreme amounts of LSP-1 were, by our criteria, as fit as the wild type. The ratio of LSP-2:LSP-1 was analyzed in 169 different stocks and was constant in 164 of these. The significantly different ratios in five stocks were all due to the lack of one of the LSP-1 gene products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499473
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  • 8
    Electronic Resource
    Electronic Resource
    AGI, a previously unreportedD. melanogaster α-glucosidase: Partial purification, characterization, and cytogenetic mapping (1996)
    Springer
    Biochemical genetics 34 (1996), S. 117-131 
    Details
    ISSN: 1573-4927
    Keywords: α-glucosidases ; Drosophila melanogaster ; carbohydrate metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract InbredDrosophila melanogaster stocks were surveyed for α-glucosidases with nondenaturing gel electrophoresis using a fluorogenic substrate to stain the gels. The glucosidase most active under these conditions is polymorphic. We established that the polymorphism is genetic in origin and that the glucosidase was not likely to be a previously characterized enzyme. The gene encoding the enzyme was mapped cytogenetically to 33 A1-2- 33A8-B1, confirming that this is an enzyme not yet reported inD. melanogaster. The enzyme was partially purified by elution from nondenaturing gels, which enabled us to establish that it has optimal activity at pH 6 and interacts most strongly with α-1–4 glucosides. A developmental and tissue survey suggested that this enzyme could have a purely digestive role or be involved in carbohydrate metabolism inside the organism. We propose that this enzyme is involved in either starch digestion or glycogen metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02396245
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  • 9
    Electronic Resource
    Electronic Resource
    AGI, a previously unreportedD. melanogaster α-glucosidase: Partial purification, characterization, and cytogenetic mapping (1996)
    Springer
    Biochemical genetics 34 (1996), S. 117-131 
    Details
    ISSN: 1573-4927
    Keywords: α-glucosidases ; Drosophila melanogaster ; carbohydrate metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract InbredDrosophila melanogaster stocks were surveyed for α-glucosidases with nondenaturing gel electrophoresis using a fluorogenic substrate to stain the gels. The glucosidase most active under these conditions is polymorphic. We established that the polymorphism is genetic in origin and that the glucosidase was not likely to be a previously characterized enzyme. The gene encoding the enzyme was mapped cytogenetically to 33 A1-2- 33A8-B1, confirming that this is an enzyme not yet reported inD. melanogaster. The enzyme was partially purified by elution from nondenaturing gels, which enabled us to establish that it has optimal activity at pH 6 and interacts most strongly with α-1–4 glucosides. A developmental and tissue survey suggested that this enzyme could have a purely digestive role or be involved in carbohydrate metabolism inside the organism. We propose that this enzyme is involved in either starch digestion or glycogen metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553608
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  • 10
    Electronic Resource
    Electronic Resource
    A comparison of the proteins found in developing wild type larvae and developing lethal mutant larvae of Drosophila melanogaster (1976)
    Springer
    Molecular genetics and genomics 148 (1976), S. 57-64 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Extracts of late larval lethal mutants were compared with extracts of wild type larvae of the same developmental age on double diffusion plates using 16 different antisera. Nearly all of the mutant extracts showed relative antigen concentration differences compared with the wild type and four of the mutants lacked a protein at death found in the wild type of the same developmental age. In each case it was a different protein. The results are discussed by considering the different ways in which mutations can lead to the loss of a protein in developing systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268546
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