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  • Calmodulin  (1)
  • DAPA, Dioxin-Panel  (1)
  • Fertilization  (1)
  • Springer  (3)
  • American Geophysical Union (AGU)
  • 1
    Electronic Resource
    Electronic Resource
    Transient recovery from trypsin-caused reduction in fertilizability of sea urchin eggs (1982)
    Springer
    Development genes and evolution 191 (1982), S. 202-204 
    Details
    ISSN: 1432-041X
    Keywords: Sperm binding ; Sea urchin eggs ; Fertilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The effect of trypsin on the fertilizability of sea urchin eggs was studied withParacentrotus lividus andPseudocentrotus depressus. The main effects were two reductions of fertilizability, with a transient increase intervening. The first decrease was probably caused by degradation of sperm-binding sites at the vitelline sheet and the second by degradation of binding sites on the plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00848336
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Lead-207 NMR: a novel probe for the study of calcium-binding proteins (1996)
    Springer
    JBIC 1 (1996), S. 39-48 
    Details
    ISSN: 1432-1327
    Keywords: Key words207Pb NMR ; Calmodulin ; Parvalbumin ; Helix-loop-helix
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The high-affinity Ca2+–binding sites of carp (pI 4.25) and pike (pI 5.0) parvalbumins, as well as those of mammalian calmodulin (CaM) and its C-terminal tryptic half-molecule (TR2C), were analyzed by 207Pb NMR spectroscopy. For the parvalbumins, two 207Pb signals were observed ranging in chemical shift from ≈750 to ≈1260 ppm downfield of aqueous Pb(NO3)2, corresponding to 207Pb2+ bound to the two high-affinity helix-loop-helix Ca2+–binding sites in each of these proteins. Four 207Pb signals, which fall in the same chemical shift window, could be discerned for CaM. Experiments on TR2C permitted the assignment of each signal as due to 207Pb2+ occupying a helix-loop-helix site in either the N- or the C-lobe of the intact protein. 207Pb and 1H NMR titration studies on CaM provided evidence that Pb2+ binding to all four sites occurs simultaneously, in contrast to the behavior of this protein in the presence of Ca2+. Titrations of the 207Pb2+–forms of CaM and TR2C with the antipsychotic drug trifluoperazine demonstrated that drug binding to the exposed hydrophobic surfaces in CaM causes substantial conformational changes and proceeds in a sequential manner – first the C-lobe and subsequently the N-lobe. Finally, the field dependence of CaM-bound 207Pb signals was examined. The 207Pb signal linewidths exhibited a sharp dependence on the square of the external magnetic field, a trend characteristic of relaxation via chemical shift anisotropy. Relaxation studies on TR2C demonstrated that chemical exchange also contributes to the observed linewidths. The large chemical shift dispersion observed for the 207Pb signals of the three proteins studied here illustrates the remarkable sensitivity of this parameter to subtle differences in the chemical environment of the protein-bound 207Pb nucleus. To our knowledge, the data presented in this article comprise the first ever published example of the application of 207Pb NMR spectroscopy to metalloproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050021
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  • 3
    Electronic Resource
    Electronic Resource
    Bestimmung von 2,3,7,8-Tetrachlordibenzo-p-dioxin in 2,4,5-Trichlorphenoxyessigsäure (1976)
    Springer
    Fresenius' Zeitschrift für analytische Chemie 280 (1976), S. 9-13 
    Details
    ISSN: 1618-2650
    Keywords: Best. von 2,3,7,8-Tetrachlordibenzo-p-dioxin in 2,4,5-Trichlorphenoxyessigsäure ; Chromatographie, Gas ; DAPA, Dioxin-Panel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Es wird eine Methode zur Bestimmung von 2,3,7,8-Tetrachlordibenzo-p-dioxin in 2,4,5-T beschrieben. 2,4,5-T wird in Dimethylformamid-Acetonitril-Wasser gelöst und mit Hexan extrahiert. Der Extrakt wird säulen-chromatographisch an Aluminiumoxid und dünnschicht-chromatographisch an Kieselgel gereinigt. Die quantitative Bestimmung des Dioxins erfolgt gas-chromatographisch auf einer SE 30-Säule mit Hilfe eines FID. Die Wiederauffindungsrate liegt bei etwa 95%, die Nachweisgrenze bei etwa 0,03 ppm. Die vom Dioxin-Panel erarbeitete Methode wurde in zwei Ringversuchen getestet.
    Notes: Abstract 2.4.5-T is dissolved in dimethylformamide-acetonitrile-water, and extracted with hexane. The extract is purified by chromatography in a column of alumina, followed by thin-layer chromatography on silicagel. The quantitative determination of dioxin is achieved by gas-liquid chromatography on a column containing SE 30 with flame-ionization detection. Recovery of dioxin is about 95%, limit of detection about 0.03 ppm. The method of the dioxin panel was tested in two collaborative studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00443540
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