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15 results on '"D. von Wachtendonk"'

1. Abstracts

Author

H. Miethke, H. Klostermeyer, E. Coduro, U. Werner, H. Steinhart, U. Engelhardt, K. Herrmann, E. Schwerdtfeger, S. Brauckhoff, B. Tofern, U. Hener, S. Wegner-Hambloch, R. Schrödter, T. Simat, J. Griffig, B. van Wickern, D. von Wachtendonk, B. Pabel, H. Scherz, A. Renger, U. Hagenauer-Hener, S. Meyer, W. Feldheim, W. Reiners, R. Galensa, C. Jahn, S. Hartmann, E. Männlein, M. Manthey, H. Karl, R. Wittmann, T. Täubert, I. Stumm, A. Täufel, J. Oehlenschläger, M. Köhnlein, A. Paschke, W. Hein, D. Ehlermann, F. Schynowski, S. Schlüter, B. Müller, M. Timm, D. Beil, R. Wedekind, H. Schulz, G. Lehmann, H. Zorn, J. Rei, M. Besler, A. Rohrdanz, T. Rathjen, M. Möller, G. von Rymon Lipinski, M. Lederer, J. Karg, M. Sengl, P. Seulen, U. Bauer, P. Majerus, L. Rothenbücher, W. Armbruster, J. Wettach, J. Hild, J. Vogelgesang, U. Wölwer-Rieck, H. van Lishaut, D. Hübner, T. Broschard, B. Carstensen, D. Breithaupt, B. Brüger, M. Kohl-Himmelseher, A. Bartsch, M. Lacorn, R. Schubring, J. Fritsche, H. Otteneder, O. Endres, H. Hahn, H. Rohse, K. Pfaff, B. Gutmacher, A. Stephani, C. Schmidt, and U. Krings

Subjects
General Chemistry, Biochemistry, Industrial and Manufacturing Engineering, Food Science, Biotechnology
Published
1996
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2. Abstracts

Author

B. Tofern, T. Simat, H. Schulz, D. von Wachtendonk, H. Wischmann, S. Schlüter, D. Beil, K. Eulitz, null Miethke, K. Herrmann, H. Rehbein, R. Wittmann, S. Wegner-Hambloch, B. van Wickern, M. Besler, H. Steinhart, J. Fritsche, A. Täufel, U. Hener, B. Pabel, W. Reiners, W. Hein, E. Schwerdtfeger, H. Spiegel, E. Männlein, I. Haselein, J. Oehlenschläger, J. Griffig, I. Stumm, H. Karl, E. Krause, G. Reinders, T. Täubert, B. Heimhuber, B. Fretzdorff, S. Hartmann, S. Bezkorovainy, D. Hübner, A. Renger, M. Schindler, W. Feldheim, T. Broschard, T. Rathjen, G. von Rymon Lipinski, M. Jager, M. Honikel, J. Reiß, E. Lück, J. Vogelgesang, M. Timm, M. Möller, W. Armbruster, U. Gasser, P. A. Kettrup, U. Bauer, J. J. Food, J. Kotoucek, M. Köhnlein, J. Wettach, H. van Lishaut, P. Majerus, S. Brauckhoff, C. Hees, H. Otteneder, T. Rudolph, M. Lederer, D. Breithaupt, U. Wölwer-Rieck, K. D. Petridis, R. Brockmann, W. Luckas B., A. Rohrdanz, O. Endres, R. Schubring, U. Engelhardt, U. Krings, C. Schulz, R. Wedekind, F. Bohnenstengel, M. Kohl-Himmelseher, A. Bartsch, F. Marx, R. Schrödter, D. Stauff, A. Paschke, N. Martin, H. Hahn, U. Hagenauer-Hener, U. Mätzel, A. Stephani, B. Gutmacher, W. Schwack, D. Ehlermann, J. Öehlenschläger, and P. Seulen

Subjects
General Chemistry, Biochemistry, Industrial and Manufacturing Engineering, Food Science, Biotechnology
Published
1996
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3. Abstracts

Author

U. Hagenauer-Hener, U. Engelhardt, L. Kroh, H. Schulz, E. Schwerdtfeger, K. Herrmann, D. von Wachtendonk, H. Steinhart, K. Eulitz, M. Möller, U. Hener, M. Besler, T. Simat, B. van Wickern, C. Schulz, W. Feldheim, H. Scherz, null Miethke, M. Manthey, B. Carstensen, N. Dillhage, J. Fritsche, E. Männlein, S. Wegner-Hambloch, B. Pabel, S. Pabel, W. Reiners, B. Heimhuber, T. Knerr, A. Renger, A. Täufel, T. Rathjen, T. Täubert, M. Timm, H. Otteneder, D. Hübner, T. Broschard, W. Hein, H. Zorn, H. van Lishaut, M. Kohl-Himmelseher, J. Reiß, S. Meyer, S. Schlüter, U. Mätzel, B. Brüger, S. Hartmann, C. Hees, P. Majerus, D. Beil, D. Breithaupt, M. Ledereraf, P. Seulen, J. Hild, J. Griffig, R. Wittmann, W. Armbruster, U. Wölwer-Rieck, M. Köhnlein, J. Wettach, M. Sengl, U. Bauer, A. Rohrdanz, F. Schynowski, J. Vogelgesang, U. Werner, A. Paschke, H. Spiegel, A. Bartsch, F. Bohnenstengel, I. Haselein, J. Karg, R. Brockmann, R. Schubring, B. Fretzdorff, Thomas Simat, F. Marx, O. Endres, H. Wischmann, Chr Schulz, R. Wedekind, K. Pfaff, A. Stephani, H. Raddatz, D. Ehlermann, H. Hahn, H. Rohse, and U. Krings

Subjects
General Chemistry, Biochemistry, Industrial and Manufacturing Engineering, Food Science, Biotechnology
Published
1996
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4. Bildung und Abbau Phenolischer Verbindungen bei einer Mikrobiologischen Bodensanierung

Author

H. G. Ebner, D. von Wachtendonk, P. Bröcking, and B. Sprenger

Abstract

Bei Bodenaushubarbeiten zur Erstellung eines offentlichen Gebaudes wurden teerolkontaminierte Bodenbereiche zutage gefordert, die aufgrund ihres hohen Schadstoffgehaltes nicht auf offentliche Deponien verbracht werden konnten. Da nur oganische Schadstoffe vorlagen (vor allem Kohlenwasserstoffe, Phenole und polycyclische aromatische Kohlenwasserstoffe), bot sich eine mikrobiologische Bodensanierung an. Wegen des hohen Anteils an Schluff und Ton erwiesen sich IN-SITU-, ON SITE- und landfarming-Methoden als unbrauchbar, da sich die Bodenkapillaren nach kurzer Zeit zusetzten und sowohl die Sauerstoffdiffusion als auch Nahrstofftransporte erschwert oder verhindert wurden. Bei der Verwendung eines Rollreaktors zur besseren Durchmischung und Beluftung wahrend des aeroben Abbaus der organischen Schadstoffe im Boden zeigte sich dabei zunachst ein Absinken, spater dann wieder ein Anstieg der Phenolkonzentration im Behandlungswasser der behandelten Boden. Die Ursache fur dieses Phanomen wird nachfolgend beschrieben.

Published
1990
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5. Amino acids and biogenic amines in smooth muscles and hemolymphs of different molluscs

Author

M. Käppler and D. von Wachtendonk

Subjects
Male, Tryptamine, Biogenic Amines, Serotonin, Taurine, Sarcosine, Immunology, Glycine, Biology, Butyric acid, chemistry.chemical_compound, Glutamates, Hemolymph, Horseshoe Crabs, Animals, Amino Acids, Arthropods, gamma-Aminobutyric Acid, Pharmacology, chemistry.chemical_classification, Muscle, Smooth, Helix pomatia, biology.organism_classification, Electric Stimulation, Amino acid, chemistry, Biochemistry, Mollusca, Putrescine, Penis
Abstract

1. Microchromatography of dansyl compounds on 3 × 3 cm polyamide sheets was used to study the distribution of amino acids and biogenic amines in smooth muscles and hemolymps of the king crab and some molluscs. 2. Using liquid scintillation counting, the amounts of glycine, glutamic acid, γ-amino butyric acid and 5-hydroxytryptamine was quantitatively determined. 3. After stimulation of the penis retractor muscle (PRM), a smooth muscle in the mollusc Helix pomatia, variations of the concentrations of these putative neurotransmitters were quantitatively determined and compared with an untreated PRM. 4. Only in the marine mollusc, Mytilus edulis, large amounts of free amino acids and taurine were detected; all other tissues and hemolymphs of the other animals examined contained essentially less free amino acids. 5. Some rare compounds could be identified in a few tissues or hemolymphs: sarcosine, ethanolamine, putrescine and tryptamine. The occurrence of free choline has not been clearly indicated. 6. The significance of these experiments has been briefly discussed.

Published
1977
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6. Evidence for serotonin (5-hydroxytryptamine) as transmitter in the penis retractor muscle ofHelix pomatia L

Author

D. von Wachtendonk and R. W. Wabnitz

Subjects
Pharmacology, medicine.medical_specialty, viruses, virus diseases, Cell Biology, Biology, humanities, Retractor, Cellular and Molecular Neuroscience, Endocrinology, medicine.anatomical_structure, Internal medicine, medicine, Molecular Medicine, Serotonin, Molecular Biology, Penis
Abstract

Microchromatography of dansylated substances was used to estimate the serotonin content of the penis retractor muscle (PRM) ofHelix pomatia. Pharmacological data in connection with the biochemical results suggest that 5-HT plays a role in the regulation of the mechanical activity of the PRM.

Published
1976
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7. Preparation and properties of acetylcholinesterase from the sea mussel Mytilus edulis

Author

H Engels, D von Wachtendonk, and Jutta Neef

Subjects
Macromolecular Substances, Protein Conformation, Iron, Carbohydrates, Immunoelectrophoresis, Biochemistry, Chromatography, Affinity, chemistry.chemical_compound, Affinity chromatography, Hemolymph, medicine, Animals, chemistry.chemical_classification, Chromatography, biology, medicine.diagnostic_test, Chemistry, Isoelectric focusing, Circular Dichroism, biology.organism_classification, Enzyme assay, Mytilus, Amino acid, Sialic acid, Bivalvia, Molecular Weight, Isoelectric point, biology.protein, Acetylcholinesterase
Abstract

The large-scale isolation of an acetylcholinesterase from the haemolymph of the sea mussel mytilus edulis by means of fractional (NH4)2SO4 precipitation, affinity chromatography and isoelectric focusing is described. The yield is about 20% of the initial enzyme activity with a specific activity of 1727 nkat/mg protein. Purification steps are followed by disc electrophoresis, analytical isoelectric focusing and immunoelectrophoresis, showing the enzyme to be homogeneous with an isoelectric point of 4.81 +/- 0.02 and to have an apparent molecular weight of 245,000, which is composed by six equal subunits as judged by C- and N-terminal amino acid analysis. The acetylcholinesterase is a metalloprotein containing three Fe2 ions per subunit (molecular weight 40625); this consists of 351 amino acid and six sugar residues, but contains no sialic acid. As calculated from CD data, the enzyme has about 55% helical structure.

Published
1978

8. [Occurrence of an acetylcholinesterase (E.C. 3.1.1.7) in the haemolymph of the mussel Mytilus edulis (author's transl)]

Author

D, von Wachtendonk

Subjects
Structure-Activity Relationship, Tetraisopropylpyrophosphamide, Acetylthiocholine, Hemolymph, Physostigmine, Acetylcholinesterase, Animals, Benzenaminium, 4,4'-(3-oxo-1,5-pentanediyl)bis(N,N-dimethyl-N-2-propenyl-), Dibromide, Neostigmine, Salicylates, Bivalvia
Abstract

A cholinesterase deriving from the hemolymph of the mussel Mytilus edulis was partially purified by use of gel-permeation and ion-exchange chromatography; the specifity to different substrates or inhibitors indicates clearly the occurrence of a "true" acetylcholinesterase.

Published
1976

10. Isolation, purification and molecular properties of an acetylcholinesterase (e.c. 3.1.1.7) from the haemolymph of the sea mussel Mytilus edulis.

Author

von Wachtendonk D and Neef J

Subjects
Acetylcholinesterase analysis, Amino Acids analysis, Ammonium Sulfate, Animals, Chemical Precipitation, Chromatography, Gel, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Acetylcholinesterase isolation & purification, Bivalvia enzymology, Hemolymph enzymology
Published
1979
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12. Preparation and properties of acetylcholinesterase from the sea mussel Mytilus edulis.

Author

Engels H, Neef J, and von Wachtendonk D

Subjects
Animals, Carbohydrates analysis, Chromatography, Affinity, Circular Dichroism, Hemolymph enzymology, Immunoelectrophoresis, Iron analysis, Macromolecular Substances, Molecular Weight, Protein Conformation, Acetylcholinesterase isolation & purification, Bivalvia enzymology
Abstract

The large-scale isolation of an acetylcholinesterase from the haemolymph of the sea mussel mytilus edulis by means of fractional (NH4)2SO4 precipitation, affinity chromatography and isoelectric focusing is described. The yield is about 20% of the initial enzyme activity with a specific activity of 1727 nkat/mg protein. Purification steps are followed by disc electrophoresis, analytical isoelectric focusing and immunoelectrophoresis, showing the enzyme to be homogeneous with an isoelectric point of 4.81 +/- 0.02 and to have an apparent molecular weight of 245,000, which is composed by six equal subunits as judged by C- and N-terminal amino acid analysis. The acetylcholinesterase is a metalloprotein containing three Fe2 ions per subunit (molecular weight 40625); this consists of 351 amino acid and six sugar residues, but contains no sialic acid. As calculated from CD data, the enzyme has about 55% helical structure.

Published
1978
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13. Influence of ions and chelating agents on the haemolymphacetylcholinesterase of Mytilus edulis.

Author

von Wachtendonk D and Neef J

Subjects
Animals, Bivalvia enzymology, Cations, Divalent, Iron analysis, Kinetics, Acetylcholinesterase metabolism, Hemolymph enzymology
Abstract

By use of different inhibitors as well as atomic absorption spectrophotometry it has been shown that the haemolymph-acetylcholinesterase (E. c. 3.1.1.7) of the sea mussel Mytilus edulis is a metalloprotein containing 2,95 Fe2+-ions per subunit. All inhibitors used (1,10-phenanthroline, salicylic aldehyde, 2,2'-dipyridyl, 8-hydroxyquinoline) showed a non-competitive inhibition, which was not pH-dependent. Some divalent cations caused a marked increase of the enzyme activity, some heavy metals inhibited the enzyme almost completely; monovalent inorganic cations did not influence the enzyme at all. Besides NaF and Na2SiF6, which showed a non-competitive inhibition comparable to the inhibition observed with the chelating agents, and NaN3, whose mode of action was not identifiable, no inhibition by different mono- and divalent inorganic anions was to be observed. Ammonium ions caused no enzyme inhibition, but length the inhibition power of substituted ammonium ions increased with an increasing C-chain. The influence of some organic solvents on the enzyme activity is demonstrated.

Published
1978
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15. [Occurrence of an acetylcholinesterase (E.C. 3.1.1.7) in the haemolymph of the mussel Mytilus edulis (author's transl)].

Author

von Wachtendonk D

Subjects
Acetylcholinesterase metabolism, Acetylthiocholine metabolism, Animals, Benzenaminium, 4,4'-(3-oxo-1,5-pentanediyl)bis(N,N-dimethyl-N-2-propenyl-), Dibromide pharmacology, Neostigmine pharmacology, Physostigmine pharmacology, Salicylates pharmacology, Structure-Activity Relationship, Tetraisopropylpyrophosphamide pharmacology, Acetylcholinesterase isolation & purification, Bivalvia enzymology, Hemolymph enzymology
Abstract

A cholinesterase deriving from the hemolymph of the mussel Mytilus edulis was partially purified by use of gel-permeation and ion-exchange chromatography; the specifity to different substrates or inhibitors indicates clearly the occurrence of a "true" acetylcholinesterase.

Published
1976

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