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  • Guinea pig  (2)
  • single strand conformation polymorphism  (2)
  • 1
    ISSN: 0006-291X
    Schlagwort(e): (ASO) ; (PCR) ; (RFLP) ; (SSCP) ; (TTR) ; allele-specific oligonucleotide ; polymerase chain reaction ; restriction fragment length polymorphism ; single strand conformation polymorphism ; transthyretin
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 0006-291X
    Schlagwort(e): (ASO) ; (PCR) ; (RFLP) ; (SSCP) ; (TTR) ; allele-specific oligonucleotide ; polymerase chain reaction ; restriction fragment length polymorphism ; single strand conformation polymorphism ; transthyretin
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    ISSN: 1432-0878
    Schlagwort(e): Ca++-ATPase ; K+-NPPase ; Na+-K+ATPase ; Ultracytochemistry ; Photoreceptor cells, retinal ; Guinea pig
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary Ca++-ATPase activity was demonstrated histochemically at light- and electron-microscopic levels in inner and outer segments of retinal photoreceptor cells of the guinea pig with the use of a newly developed one-step lead-citrate method (Ando et al. 1981). The localization of ouabain-sensitive, K+-dependent p-nitrophenylphosphatase (K+-NPPase) activity, which represents the second dephosphorylative step of the Na+-K+-ATPase system, was studied by use of the one-step method newly adapted for ultracytochemistry (Mayahara et al. 1980). In retinal photoreceptor cells fixed for 15 min in 2% paraformaldehyde the electron-dense Ca++-ATPase reaction product accumulated significantly on the inner membranes of the mitochondria but not on the plasmalemma or other cytoplasmic elements of the inner segments. The membranes of the outer segments remained unstained except the membrane arrays in close apposition to the retinal pigment epithelium. The cytochemical reaction was Ca++- and substrate-dependent and showed sensitivity to oligomycin. When Mg++-ions were used instead of Ca++-ions, a distinct reaction was also found on mitochondrial inner membranes. In contrast to the localization of the Ca++ -ATPase activity, the K+-NPPase activity was demonstrated only on the plasmalemma of the inner segments, but not on the mitochondria, other cytoplasmic elements or the outer segment membranes. This reaction was almost completely abolished by ouabain or by elimination of K+ from the incubation medium.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Cell & tissue research 237 (1984), S. 491-497 
    ISSN: 1432-0878
    Schlagwort(e): CA++-ATPase ; Pituitary gland, pars nervosa ; Pituicytes ; Neurosecretion ; Guinea pig
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary Ca++-ATPase activity (cf. Ando et al. 1981) was examined both light- and electron-microscopically in the neurohypophysis of the guinea pig. Apart from a strong activity within the walls of the blood vessels, in the parenchyma of the neurohypophysis the reaction product of the Ca++-ATPase activity was restricted to the plasmalemma of the pituicytes. This reaction was completely dependent upon Ca++ and the substrate, ATP; the reaction was inhibited by 0.1 mM quercetin, an inhibitor of Ca++-ATPase. A reduction of the enzyme activity occurred by 1) adding Mg++ to the standard incubation medium, and 2) substituting Ca++ with Mg++ at varing concentrations. In all experiments the neurosecretory fibers were devoid of Ca++-ATPase activity. The function of the Ca++-ATPase activity in the plasmalemma of the pituicytes is discussed in connection with the regulation of the extracellular Ca++ concentration, which seems to be important with respect to the discharge of secretory material from the neurosecretory fibers.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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