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  • Spektralphotometrie  (58)
  • Drosophila melanogaster
  • Springer  (74)
  • American Association for the Advancement of Science
  • Nature Publishing Group
  • 1970-1974  (74)
Collection
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  • Springer  (74)
  • American Association for the Advancement of Science
  • Nature Publishing Group
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 11 (1974), S. 167-175 
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; conformers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two isozymes of alcohol dehydrogenase from Drosophila melanogaster homozygous for the Adh-slow allele have been separated by isoelectric focusing. The isozymes differ in their temperature optima, temperature stabilities, specific activities, and at least one of their Michaelis constants. They are immunologically identical. Evidence is presented that NAD may partially convert one isozyme into another. The possible nature of these isozymic differences is discussed.
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  • 2
    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.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 11 (1974), S. 177-180 
    ISSN: 1573-4927
    Keywords: alkaline phosphatase ; Drosophila melanogaster ; tyrosine-O-phosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Tyrosine-O-phosphate was used as a substrate for two allelic forms (APH-4 and-6) of alkaline phosphatase of late third instar larvae of Drosophila melanogaster. Two findings of particular interest are (1) lack of inhibition by 1mm inorganic phosphate and (2) severe substrate inhibition. The accumulated evidence that, in vivo, alkaline phosphatase catalyzes the conversion of tyrosine-O-phosphate into tyrosine, which is then utilized for puparium formation, is discussed.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 11 (1974), S. 141-153 
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; allozymes ; polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Studies of the isozymes produced by alternative alleles at the alcohol dehydrogenase locus of Drosophila melanogaster indicate that the ADH F enzyme is more active but less stable than the ADHS enzyme. The difference in stability is manifested in the responses to various conditions of temperature, pH, and protein concentration. The two enzymes also appear to differ in their substrate specificities. It is clear that the differences of primary structure involved in the ADH polymorphism can have profound effects on the biological activity of the molecule.
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  • 5
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; enzyme kinetics ; polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have examined the kinetic properties of enzymes produced by the electrophoretically fast (F) and slow (S) alleles at the alcohol dehydrogenase locus in a polymorphic laboratory population of Drosophila melanogaster. The product of the F allele has approximately twice the specific activity of the product of the S allele. We have estimated four Michaelis constants (K ethanol, K NAD, K′ethanol, and K′NAD) and have found no significant difference between the major (ADH-5) isozyme produced by homozygotes for the two alleles. The relative amounts of enzyme produced by the homozygotes were estimated by the method of Laurell (1966), and again no significant differences were found. It appears that the difference in specific activities can be explained solely in terms of relative catalytic efficiency. In a series of laboratory stocks, those fixed for the F allele tend to produce more enzyme than those fixed for the S allele. These observations do not support the view that the alleles are selectively equivalent.
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  • 6
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; Drosophila simulans ; interspecific hybrids ; esterases ; regulation by X chromosome in Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The present report presents the results of starch and polyacrylamide gel electrophoretic studies of the influence of the X chromosome on the expression of esterase-6 in D. melanogaster × D. simulans hybrids heterozygous for locus Est-6 as well as studies of the influence of autosomes on esterase expression in Drosophila of the virilis group. A differential expression of esterase-6 has been detected in D. melanogaster × D. simulans hybrid males. A differential decrease in the activity of esterase-6 (both F and S allozymes) derived from D. melanogaster has been noted. In hybrid females, the activity of parental esterases is the same. It is suggested that the X chromosome regulates the expression of esterase-6 in D. melanogaster. Analysis of individuals obtained in different schemes of crosses between different species of Drosophila of the virilis group by use of stocks marked with mutations in various chromosomes indicates that other autosomes (in particular, autosomes 4 and 5) also influence the phenotypic expression of esterases (which are controlled by genes located on the second chromosome).
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 12 (1974), S. 449-458 
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; protein polymorphism ; allozymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A natural population of Drosophila melanogaster was examined for activity variation in the polymorphic enzyme alcohol dehydrogenase. The overall mean activity of the ADH-F strains proved to be approximately twice that of the ADH-S strains. Within each of the two electrophoretic classes, there was a wide spread of activity values and some overlap in activity between the classes. This variation should be taken into account when discussing the functional significance of the electrophoretically detectable polymorphism.
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  • 8
    Electronic Resource
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    Springer
    Cell & tissue research 131 (1972), S. 269-286 
    ISSN: 1432-0878
    Keywords: Drosophila melanogaster ; Renal tubules ; Fine structure and function ; Localization of sodium and chloride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Diese Untersuchung beschreibt die Lokalisation von Natrium- und Chloridionen in den Zellen der verschiedenen Regionen der Malpighischen Gefäße von Drosophila melanogaster. Bezüglich der Lokalisation bestehen zwischen den Zellen des Anfangsstückes und des Hauptstückes Unterschiede. Einen Überblick über die Ergebnisse zeigt eine schematische Darstellung (Abb. 7). Die Ergebnisse werden eingehend diskutiert.
    Notes: Summary The localization of sodium and chloride ions in cells of the different regions of the Malpighian tubules in the larvae of Drosophila melanogaster is described. There are ultrastructural differences between the cells of the initial region and the cells of the main region of the tubules. The results are demonstrated in a schematic drawing (Fig. 7) and are discussed in detail.
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  • 9
    Electronic Resource
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    Springer
    Cell & tissue research 133 (1972), S. 119-130 
    ISSN: 1432-0878
    Keywords: Renal tubules ; Drosophila melanogaster ; Fine structure ; Localization of adenosine triphosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Die vorliegende Studie behandelt die Lokalisation von Adenosintriphosphatase an den Feinstrukturen der Malpighischen Gefäße der Larven von Drosophila melanogaster. In den Zellen des Anfangs- und Hauptstückes zeigt sich zum Lumen hin eine Aktivitätszunahme des Enzyms. Es kommt nicht frei im Cytoplasma vor, sondern ist stets an Membranstrukturen gebunden; man findet es am basalen Plasmalemm mit seinen Einfaltungen, am endoplasmatischen Retikulum, an Vesikeln, in multivesikulären Körpern und — besonders deutlich — an den Membranen der Mikrovilli, die in das Gefäßlumen hineinragen. Die Ergebnisse werden in einem Schema (Abb. 5b, c) wiedergegeben und mit den Befunden der Na+-Lokalisation (Wessing und Eichelberg, 1972b) verglichen.
    Notes: Summary This paper describes the localization of adenosine triphosphatase within certain ultrastructural elements of the cells of the initial and main regions of the Malpighian tubules of Drosophila melanogaster larvae. In both regions, an increased activity is observed towards the lumen. The enzyme is always related to such membrane structures as the basement membrane (especially its infolds), vesicles, multivesicular bodies, and densely to microvilli which projects towards the lumen of the renal tubules. The results (presented in a schematic drawing in Fig. 5b and c) are discussed in relation to those on Na+-localization (Wessing and Eichelberg, 1972b).
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 136 (1973), S. 415-432 
    ISSN: 1432-0878
    Keywords: Drosophila melanogaster ; Rectal papillae ; Fine structure and function ; Localization of Na+ and Cl− ions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Die Zellen der vier Rektalpapillen von Drosophila melanogaster sind polar gebaute, hochdifferenzierte, transportaktive Zellen mit großflächigen Ein- und Ausfaltungen des Plasmalemms. Ihre basale und laterale Zellmembran bildet ein Netzwerk von Einfaltungen, aus dem zahlreiche Stapel von Membranpaaren hervorgehen, die mit Mitochondrien vergesellschaftet sind. Apikal besitzt die Zelle ein System von Mikroleisten, an deren Basis ebenfalls Mitochondrien akkumuliert sind (s. Abb. 9). Bei Drosophila werden nach Durchführung der entsprechenden elektronenmikroskopischen Nachweise Natriumionen an den Membranen der apikalen Ausfaltungen, an den Membranen der interzellulären Stapel der Membranpaare, innerhalb deren Lumina und in den basalen und lateralen Einfaltungen gefunden. Eine bevorzugte Lokalisation von Chloridionen ist nicht vorhanden. Diese Feinstrukturaspekte und die Ergebnisse der Nachweisreaktionen für Natrium und Chloridionen werden mit den Verhältnissen bei Calliphora erythrocephala (Gupta und Berridge, 1966) verglichen und die Transportwege der Ionen eingehend diskutiert.
    Notes: Summary In Drosophila melanogaster the cells of the rectal papillae are highly differentiated and very active in transport. These cells show extensive infoldings of the plasmalemma. The basal and lateral cell membranes form a system of infoldings, continuous with intracellular stacks of paired membranes which are associated with mitochondria. The apex of the cell displays a system of micro-ridges with basal mitochondria (see Fig. 9). In Drosophila Na+ ions can be demonstrated by electron microscopy at the membranes of the apical micro-ridges, at the membranes and within the lumina of the intracellular stacks of paired membranes, and within the basal and lateral infoldings. In contrast, there is no predominant localization of Cl− ions. The fine structure of the cells of the rectal papillae and the results of cytochemical demonstration of Na+ and Cl− ions are compared with the findings of Gupta and Berridge (1966) in Calliphora erythrocephala. The possible pathways for ion transport are discussed in detail.
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