Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
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Volume 37, Issue 2
Displaying 1-8 of 8 articles from this issue
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  • Mechanism for intracellular localization of cytochrome P450
    Masao SAKAGUCHI
    1997Volume 37Issue 2 Pages 52-57
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.52
    JOURNAL FREE ACCESS
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    Different molecular species of cytochrome P450 exist in two intracellular organella, the endoplasmic reticulum and mitochondria in eukaryotic cells. Microsomal P450s possess uncleavable signal sequences whose orientation in the membrane is inverted to the signal peptides of secretory proteins. Their unique function is dependent on the balance between the hydrophobic segment and its amino-terminal charges. Mitochondrial P450s possess extension peptides which target the precursor molecules to mitochondria. The precursors are recognized, kept in an import competent state, and targeted to mitochondria by mitochondrial import stimulation factor (MSF).
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  • Mitosis, microtubules and γ-tubulin.
    Tetsuya HORIO
    1997Volume 37Issue 2 Pages 58-62
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.58
    JOURNAL FREE ACCESS
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    Microtubules are dynamic and multifunctional organelles, which are mainly composed of α and β-tubulin. γ-Tubulin is a recently identifed member of tubulin gene superfamily. Unlike its counterparts, γ-tubulin localizes at microtubule organizing centers and play an essential role in nucleating microtubules. Recently, protein complex containing γ-tubulin has been purified from Xenopus egg extract. This ring-like structure containing γ-tubulin is considered to be the long-sought-after microtubule nucleating complex.
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  • Three-dimensional structure of bacterial flagellar motor in the cytoplasmic membrane
    Eisaku KATAYAMA, Shin-Ichi AIZAWA, Kenji OOSAWA
    1997Volume 37Issue 2 Pages 63-67
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.63
    JOURNAL FREE ACCESS
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    The three-dimensional molecular architecture of Salmonella flagellar motor in the bacterial membrane was examined in situ, by quick-freeze deep-etch replica electron microscopy. The MS ring complex, the FliF gene product, which was over-expressed in E. coli appeared as a drilled bead sitting on a flat disk, projecting toward the periplasm. The cytoplasmic side of the intact flagella consisted of a large bell-shaped structure, which was identified to C ring. In its center, we found a new rod-like structure with a central hole, which we denominated as C rod. This structure may operate as an apparatus to selectively transport the flagellar proteins across the membrane.
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  • The world fastest myosin form Chara corallina
    Keiichi YAMAMOTO
    1997Volume 37Issue 2 Pages 68-72
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.68
    JOURNAL FREE ACCESS
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    Cytoplasmic streaming is a fundamental process for the transport of molecules and organelles in plant cells. A myosin-like protein responsible for cytoplasmic streaming in fresh water alga, Chara corallina, has been purified. Electron micrographs of this protein revealed that it has two heads with similar size and shape to those of muscle myosin (myosin II) but its tail is shorter than that of muscle myosin with a globular structure at its distal end like that of myosin V.
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  • Hemolytic properties of human erythrocytes under hydrostatic pressure
    Takeo YAMAGUCHI
    1997Volume 37Issue 2 Pages 73-77
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.73
    JOURNAL FREE ACCESS
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    Membrane structure of human erythrocytes has been intensively studied as a prototype of biological membranes. However, it is not well elucidated about the interactions between membrane components such as membrane proteins and phospholipids. As compared with hypotonic hemolysis, high pressure-induced hemolysis is very sensitive to chemical or enzymatic modification of membrane proteins. The present paper describes that the high pressure technique provides unique information about an investigation of membrane structure.
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  • A standing wave of chemical reaction on the skin of animals
    Turing wave as the chemical basis of morphogenesis
    Shigeru KONDO
    1997Volume 37Issue 2 Pages 78-80
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.78
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  • RNA-primed PCR
    Soichiro FURUKAWA, Hiroki SHIBATA, Kenshi HAYASHI
    1997Volume 37Issue 2 Pages 81-82
    Published: March 25, 1997
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.37.81
    JOURNAL FREE ACCESS
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  • Erratum
    1997Volume 37Issue 2 Pages e1
    Published: 1997
    Released on J-STAGE: January 07, 2010
    DOIhttps://doi.org/10.2142/biophys.37.2_e1
    JOURNAL FREE ACCESS
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