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  • Springer  (19)
  • Elsevier  (16)
  • American Physical Society  (3)
  • 1985-1989  (24)
  • 1965-1969  (14)
  • 1
    Electronic Resource
    Electronic Resource
    Siderite — a diagenetic product of an ammonite shell (1987)
    Springer
    Naturwissenschaften 74 (1987), S. 445-446 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446103
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  • 2
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    Siderite ? a diagenetic product of an ammonite shell (1987)
    Springer
    Details
    Publication Date: 1987-09-01
    Print ISSN: 0028-1042
    Electronic ISSN: 1432-1904
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Published by Springer
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    PAPER CURRENT
  • 3
    Electronic Resource
    Electronic Resource
    ESR study of Fe(III) and Cr(III) hydroxides (1989)
    Springer
    Naturwissenschaften 76 (1989), S. 172-173 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00366401
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  • 4
    Electronic Resource
    Electronic Resource
    Dimethylsulfoxyd als Extraktionsmittel für Streptokokkenantigene (1967)
    Springer
    Naturwissenschaften 54 (1967), S. 372-372 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00636647
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  • 5
    Electronic Resource
    Electronic Resource
    Synchrone Replikation aller Chromosomen beiXenopus laevis (1967)
    Springer
    Cellular and molecular life sciences 23 (1967), S. 40-41 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Autoradiographics showed synchronous replication of all chromosomes inXenopus laevis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02142257
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  • 6
    Electronic Resource
    Electronic Resource
    In situ localization of the transcripts of a homeobox gene in the honeybee Apis mellifera L. (Hymenoptera) (1988)
    Springer
    Development genes and evolution 197 (1988), S. 269-274 
    Details
    ISSN: 1432-041X
    Keywords: Apis mellifera ; Homeobox genes ; Dfd ; In situ hybridization ; Blastoderm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have isolated and characterized a homeoboxcontaining gene from the honeybee Apis mellifera. Its homeobox region shows a high degree of sequence similarity to the homeobox of the Drosophila gene Deformed (Dfd). At the DNA level 82% of the basepairs are the same, whereas the putative amino acid sequences are identical between the bee and the fruitfly genes. Similarity is also present 5′ and 3′ to the homeobox. Using this isolate as a probe we have performed in situ hybridization on sections from blastoderm-stage embryos of the honeybee Apis mellifera. In early blastoderm stages we found a rather irregular pattern of labelled nuclei. In middle stages we found silver grains over each nucleus and also over the cytoplasm in a belt of blastoderm cells in the prospective gnathal region. These results indicate that the Deformed genes from honeybee and fruitfly are homologous both with respect to their DNA sequence and their spatial and temporal pattern of expression during embryogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00380020
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  • 7
    Electronic Resource
    Electronic Resource
    Biochemische Untersuchungen zur Frage der Existenz eines “silent Gene” im Polymorphismus der Pseudocholinesterasen (1966)
    Springer
    Human genetics 〈Berlin〉 1 (1966), S. 607-620 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Zwei Seren des Phänotypus Ch1SS, die unter Standardtestbedingungen keine Pseudocholinesteraseaktivität aufwiesen, wurden mit Hilfe der Stärkegel-Elektrophorese, der Mikromanometrie und mit immunologischen Methoden näher untersucht. Nach elektrophoretischer Auftrennung läßt sich in diesen “silent gene”-Seren eine Pseudocholinesteraseaktivität nachweisen; im Vergleich zu der Aktivität von Normalserum erscheint diese sehr gering und läßt sich nur in der c4-Zone erkennen. Die Identifizierung gelingt mit Hilfe spezifischer Färbeverfahren unter Verwendung verschiedener Substrate und Inhibitoren. Die quantitative Bestimmung von Pseudocholinesteraseaktivität im “silent gene”-Serum mit mikromanometrischen Methoden ergab eine Aktivität von 2–3% gegenüber den Kontrollen (Benzoylcholin als Substrat). Durch Immunisierung von Kaninchen mit gereinigtem Pseudocholinesteraseprotein wurden Antiseren erhalten; zwischen “silent gene”-Serum und diesen Antiseren konnten Präzipitationsreaktionen im Immuno-Diffusionstest, in der Immuno-Elektrophorese und mit einer Immuno-Adsorptionsmethode nachgewiesen werden. Diese Ergebnisse lassen annehmen, daß bei den von uns untersuchten Fällen das “silent gene” im Pseudocholinesterasepolymorphismus eine Enzymproteinsynthese steuert; das nachgewiesene Pseudocholinesteraseprotein scheint sich qualitativ von dem Enzymprotein des Normalserums zu unterscheiden.
    Notes: Abstract Two sera “without” pseudocholinesterase activity corresponding to the homozygous phenotype Ch1SS are examined by electrophoretical, manometric, and immunological methods. These “silent gene” sera show no activity under the common conditions (spectrophotometric assay). After electrophoretical separation of “silent gene” serum an esterase activity is found which can be identified as pseudocholinesterase activity, although it is weak in comparison with the activity of usual sera. The pseudocholinesterase activity of “silent gene” serum can be demonstrated only in the zone “c4” where 90% of the total activity is present if usual serum is inserted. The identification has been achieved by staining procedures applying several substrates and inhibitors. Quantitative estimation of this pseudocholinesterase activity was carried out by micromanometric assays with benzoylcholine as substrate. The activity of “silent gene” sera was 2–3% of normal serum. Antisera against human pseudocholinesterase-protein have been obtained by immunization of rabbits with a highly purified enzyme protein. Between these antisera and the homozygous “silent gene” sera precipitates were found in immuno double-diffusion tests and immunoelectrophoresis. They could be identified as pseudocholinesterase protein by esterase staining under various conditions. Quantitative estimations have been carried out by immuno-adsorption assays comparing the amount of antibody fixed by usual serum and by “silent gene” serum. The results presented in this paper suggest that the “silent gene” in pseudocholinesterase polymorphism induces in these two cases the synthesis of an enzyme protein which is similar to the enzyme protein of usual pseudocholinesterase. The weak activity is due to a qualitative difference between “silent gene” enzyme protein and the normal pseudocholinesterase protein. A structural alteration of the enzyme protein is assumed to be more likely than a quantitative difference in protein synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281049
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  • 8
    Electronic Resource
    Electronic Resource
    Methoden zur Identifizierung, Anreicherung und Charakterisierung genetisch bedingter Acylcholin-Acyl-Hydrolase-Varianten (E.C. 3.1.1.8.) (1965)
    Springer
    Fresenius' Zeitschrift für analytische Chemie 212 (1965), S. 238-252 
    Details
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Es werden verschiedene Methoden zur Differenzierung genetisch bedingter Enzymvarianten der Pseudocholinesterase (spektrophotometrischer Test, Agar-Diffusionstest, Säulenchromatographie), Versuche zur Charakterisierung der verschiedenen Enzymproteine und der in der Stärkegelelektrophorese auftretenden vier Enzymfraktionen mitgeteilt. Ein Reinigungsverfahren für die Pseudocholinesterase wurde ausgearbeitet; nach der Immunisierung von Kaninchen mit dem angereicherten Enzymprotein wurden mit dem gewonnenen Antiserum immunchemische Versuche durchgeführt.
    Notes: Summary Methods are reported for the differentiation and characterisation of genetically determined enzyme variants and the enzyme fractions occuring in starch-gel electrophoresis of pseudocholinesterase (spectrophotometrical assays, agar diffusion test, column chromatography). A method has been developed to purify the pseudocholinesterase. Rabbits were immunized against a purified enzyme protein. Results of these immuno-chemical assays are given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00518367
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  • 9
    Electronic Resource
    Electronic Resource
    Excision of copia element in a revertant of the white-apricot mutation of Drosophila melanogaster leaves behind one long-terminal repeat (1985)
    Springer
    Molecular genetics and genomics 199 (1985), S. 1-6 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The spontaneous mutation white-apricot (wa) in Drosophila melanogaster has a considerably highter eye colour than the wild-type, and is caused by the insertion of a copia transposable element into a small intron of the white gene. We have analyzed an X-ray induced w a revertant (w aR59K1), whose eye pigmentation is incompletely restored, by in situ hybridization, Southern blotting and sequencing analysis. At the site where copia had originally inserted, we found one long terminal repeat of copia, flanked by a 5 bp duplication with the same polarity as the direction of transcription of the white locus. These results suggest that the w a reversion is due to homologous recombination between the two long terminal repeats of copia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327501
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  • 10
    Electronic Resource
    Electronic Resource
    On the nature of Romanowsky-Giemsa staining and the Romanowsky-Giemsa effect. I. Model experiments on the specificity of Azures B-Eosin Y stain as compared with other thiazine dye-Eosin Y combinations (1985)
    Springer
    Journal of molecular histology 17 (1985), S. 263-289 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary After incorporation into a polyacrylamide matrix, the biopolymers DNA, RNA, heparin, hyaluronic acid, collagen and the synthetic polymers poly(U) and poly(A, U) were stained with the pure thiazine dyes, Methylene Blue, the Azures and Thionin alone and combined with Eosin Y. Satisfactory spectrophotometric agreement was obtained between the staining reactions of the biopolymers in the artificial matrix and those in their natural surroundings. This was especially true with respect to the specificity of the Azure B-Eosin Y dye-pair, which is based on the generation, on suitable substrates, of a purple colour, the Romanowsky-Giemsa effect (RGE), with an absorbance maximum near 550 nm. In the model experiments, DNA, heparin, hyaluronic acid and collagen were found to be RGE-positive and poly(U), poly(A, U) and RNA RGE-negative. A theory of RGE is proposed which complies with the new and earlier observations: after saturation of available anionic binding sites and aggregate formation by Azure B, electron donor acceptor complexes are formed between Eosin Y and Azure B via hydrogen-bridge formation of the aminosubstituent proton of Azure B and between Eosin Y and the biopolymer surface. Charge-transfer complex formation may also account for the qualitative identity of Azure B-Eosin Y and Azure A-Eosin Y spectra of substrates, which are coloured purple. Quantitatively, Azure A-Eosin Y is less efficient in giving RGE. The generation of RGE is time-dependent. Equilibrium staining is attained after about 120 h. The implications of the results for the biological application of Romanowsky-Giemsa staining are discussed briefly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01004591
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