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  • 2000-2004  (3)
  • Haloarcula japonica  (2)
  • Electron microscopy
  • Immunohistochemistry
  • Life and Medical Sciences
  • [abr] BSA; bovine serum albumin
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Year
Keywords
  • 1
    ISSN: 1572-8773
    Keywords: extremely halophilic archaeon ; Haloarcula japonica ; ferredoxin ; iron-sulfur cluster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A ferredoxin (Fd) was purified from the extremely halophilic archaeon, Haloarcula japonica strain TR- 1, to electrophoretic homogeneity. The apparent molecular weight (M r) of the Fd was estimated to be 24,000 on SDS-polyacrylamide gel electrophoresis. The amino acid composition analysis revealed that the Fd composed of a number of acidic amino acids (uncorrected for amides). The N-terminal amino acid sequence (30 residues) was determined to be: PTVEYLNYEVVDDNGWDMYDDDVFAEASDM. The iron content was 3.42±0.04 mol/mol-Fd on the basis of the apparent M r value. The absorption and ESR spectra of the Fd showed similarity to those of Fds from plant and Halobacterium halobium. These results led us to conclude that the H. japonica Fd contained a [2Fe-2S] cluster.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1433-4909
    Keywords: Key words Bacteriorhodopsin ; Halophilic archaeon ; Haloarcula japonica ; Gene cloning ; Transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene encoding a novel bacteriorhodopsin (bR) -like protein from Haloarcula japonica strain TR-1 was cloned and sequenced. The nucleotide sequence of the gene contained an open reading frame that corresponded to a protein of 250 amino acids. The deduced amino acid sequence of Ha. japonica bR-like protein exhibited the highest homology to those of cruxrhodopsins (cRs) produced by members of the genus Haloarcula, suggesting that the bR-like protein of Ha. japonica belonged to the cR subfamily. The hydropathy analysis of Ha. japonica bR-like protein (cR) revealed that the Ha. japonica cR had a transmembrane heptahelical structure similar to that of bR. Furthermore, transcription of the cR gene in Ha. japonica was confirmed by the reverse transcription-polymerase chain reaction method.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Key words Glial cell line-derived neurotrophic factor ; Human cerebellum ; Immunohistochemistry ; Multiple system atrophy ; Purkinje cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Glial cell line-derived neurotrophic factor (GDNF) has a trophic effect on various types of neurons, including cerebellar Purkinje cells. To investigate the role of GDNF in the human cerebellum, we examined the cerebella of eight control cases and eight patients with multiple system atrophy (MSA) immunohistochemically using a polyclonal anti-GDNF antibody. The antibody recognized a single band of approximately 34 kDa on Western blot analysis of human cerebellar homogenates. In the cerebella from normal subjects, the neuronal somata and dendrites of the Purkinje cells were immunostained intensely, as were some axons, including torpedoes, immunolabeled in the granular layer. Many axons and a few oligodendrocytes were also immunopositive in the white matter, and weak immunoreactivity was detected in the granule cells and neurons in the cerebellar nuclei. In the cerebella from patients with MSA, the general immunostaining pattern was similar to that observed in the normal subjects. Most of the remaining Purkinje cells showed strong immunoreactivity, and abundant GDNF-positive granular structures or dense arborizations of GDNF-positive dendrites were found in some areas of the molecular layer. These data suggest that GDNF may be mainly produced and localized in the Purkinje cells of the human cerebellum, even in patients with MSA, and that the functional impairment of the Purkinje cells of MSA patients might cause a focal accumulation of GDNF in the dendrites of some of the surviving Purkinje cells.
    Type of Medium: Electronic Resource
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