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  • Electronic Resource  (6)
  • 1985-1989  (3)
  • 1950-1954  (3)
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  • Electronic Resource  (6)
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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 170 (1952), S. 1072-1073 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The nucleic acid bases liberated by hydrolysis of whole viruses or virus deoxyribonucleic acid were separated on paper chromatograms using isopro-panol - water - hydrochloric acid5 as the solvent. When formic acid (88 per cent at 175 C. for 30 min.) was used for hydrolysis, a substance was ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 170 (1952), S. 846-847 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We have recently analysed the deoxyribonucleic acid of another rickettsia from the same host. Deoxyribonucleic acid was isolated2 from epidemic typhus rickettsise (R. prowazeki) grown in chick yolk-sac endothelium, and the purine and pyrimidine bases estimated3 after hydrolysis in perchloric acid ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 166 (1950), S. 237-238 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Taking advantage of the sensitive photographic technique of Markham and Smith4 for the detection of ultra-violet-absorbing substances on paper chroma-tograms, I have now been able to demonstrate and estimate 5-methyl-cytosine in several animal and plant deoxyribonucleic acids, but not in certain ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 156 (1986), S. 813-817 
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Locusta migratoria adults reared at 27–30°C die after 2 h at 50°C, but they survive this temperature stress if first exposed to 45°C for 0.5 to 4.5 h. Fat bodies from adult females produce a set of at least six specific polypeptides with molecular weights of 81, 73, 68, 42, 28, and 24×103 in reponse to heat shock (39–47°C for 1.5 h). These molecular weights closely match those of the heat shock proteins (hsps) observed inDrosophila, with the possible exception of the 42 kd protein of locusts. The optimal temperature for induction of hsps in locusts is 45°C, which is one of the highest heat shock temperatures reported in metazoans. The correspondence between the optimal temperature for hsp induction and the temperature at which enhanced heat tolerance is acquired (both 45 °C) suggests that the hsps may be associated with thermal protection in these insects. There appears to be no substantial translational control in the locust heat shock response, since other proteins are produced, albeit with some reduction, under heat shock conditions. Vitellogenin synthesis in fat bodies at 45°C is 55% of that observed at 30°C. The high optimal heat shock induction temperature and the continued synthesis of non-heat shock proteins may be adaptive to the locust's natural environment.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 8 (1988), S. 203-217 
    ISSN: 0739-4462
    Keywords: fat body ; insect gene ; juvenile hormone ; locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: From a Locusta migratoria genomic DNA library, a gene has been isolated that codes for a previously unrecognized hemolymph protein of Mr = 19,000, designated 19k protein. The gene has at least five exons, extending over about 9 kb of DNA. Its polypeptide product, obtained by cell-free translation of mRNA selected from adult fat body RNA by hybridization with the cloned DNA, is precipitated by antiserum against a low molecular weight hemolymph protein fraction. The mature protein product has been purified from locust hemolymph, and an N-terminal sequence of 20 amino acids has been determined. In polyacrylamide gel electrophoresis, this protein comigrates with apolipophorin III, from which it was previously not distinguished, but it is clearly distinct by amino acid composition and sequence. The genomic clone was used as a probe to isolate a fat body cDNA clone of the 19k protein mRNA. The 938-base pair cDNA clone contains a 516-base pair open reading frame. The deduced 172-amino acid polypeptide includes an apparent signal peptide, a sequence of four amino acids that may represent a prosegment, and a sequence identical (with a single exception, which may reflect polymorphism) with the N-terminal sequence of the hemolymph protein. Its mRNA occurs at a low level in late larval fat body, is abundant in the newly eclosed adult, then declines to a low level, and rises again at days 8-10; it is greatly reduced after destruction of the corpora allata with precocene and then is elevated after treatment with methoprene, suggesting stimulation by juvenile hormone. The biological role of 19k protein is unknown.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 35-46 
    ISSN: 0739-4462
    Keywords: locust ; vitellogenin ; juvenile hormone ; P element ; Drosophila ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In Locusta migratoria, vitellogenin (Vg) is normally produced only in adult female fat body under stimulation by juvenile hormone (JH). This permits study of (a) programming of genes for expression and (b) modulation of expression by JH. From L. migratoria genomic libraries, two Vg genes (A and B) have been cloned. Coding regions encompass 10-12 kbases of DNA, contain introns, and hybridize with 6,300 nucleotide mRNAs. Although the 5'-exons, coding for signal peptides, are similar in sequence, the remaining coding sequences have distinct restriction maps and show no crosshybridization. Upstream DNA from the two genes has some sequence similarity, corresponding to potential regulatory regions. Dot hybridization assays of mRNAs A and B in locust fat body after induction by methoprene show coordinate expression of the two Vg genes and also a third, unidentified JH-regulated gene. In the hope of providing a system for identification of control sequences, P element-mediated transformation has been used to transfer locust DNA into Drosophila. From Vg gene B, a central block was deleted, to give a mini-Vg gene comprising 5' and 3' terminal coding sequences plus upstream flanking DNA. This was incorporated into the P element vector Carnegie 20 and injected into Drosophila embryos. Three transformed fly lines were obtained in which the locust mini-Vg gene was integrated at different chromosomal sites. On Northern blots of fly RNA, however, no expression of the locust sequences could be detected, even though the accompanying rosy gene was expressed. This suggests that the locust regulatory sequences were not recognized in Drosophila, and current effort is directed toward developing a homologous locust transformation system for expression assay of cloned JH-regulated genes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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