Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
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Volume 28, Issue 2
Displaying 1-11 of 11 articles from this issue
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  • Characteristic features of protein coding regions in DNA
    From the viewpoint of thermal stability map
    Ryo HANAI, Akiyoshi WADA, Akira SUYAMA
    1988 Volume 28 Issue 2 Pages 57-60
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.57
    JOURNAL FREE ACCESS
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    Resonance of physical and biological aspects of DNA is reviewed. Thermal stability map of DNA has revealed that protein coding region has an inclination to have uniform stability, i.e., gene homostabilizing propensity, and that discontinuities of thermal stability with protein coding regions are vestiges of introns.
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  • Folding units in protein structures and Correlations with intron positions
    Shin-ichi SEGAWA
    1988 Volume 28 Issue 2 Pages 61-63
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.61
    JOURNAL FREE ACCESS
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    An algorithm has been developed to estimate flexibility for potential hinge motion at specified residues. The first step of unfolding is likely to occur at the hinge point with the largest flexibility. Sequence flexibility charts are discussed for cytochrome c and lysozyme. Some well-isolated hinges were found to be directly at or close to the intron positions.
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  • ∅X174 DNA replication and Phage Morphogenesis
    Akira AOYAMA
    1988 Volume 28 Issue 2 Pages 64-69
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.64
    JOURNAL FREE ACCESS
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    In the late stage of infection, the morphogenetic reaction of bacteriophage ∅X174 is switched from DNA replication mode to phage formation mode by the function of ∅X174 gene C protein, gene J protein, and prohead. During the phage synthesis, structural changes of the capsid-related proteins occur. The gene B protein of prohead is cleaved at a specific site by a novel protease which has been isolated from the outer membrane of Escherichia coli cells. Cross-linking experiments indicate that the rearrangement of gene F major coat proteins occurs during DNA packaging.
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  • Chromosome Translocations in Human B-Cell Neoplasms
    Yoshihide TSUJIMOTO
    1988 Volume 28 Issue 2 Pages 70-76
    Published: March 25, 1988
    Released on J-STAGE: January 07, 2010
    DOIhttps://doi.org/10.2142/biophys.28.70
    JOURNAL FREE ACCESS
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    It is generally accepted that tumors arise through the accumulation of several genetic changes affecting the control of cell growth. To date, the best characterized of these changes are the chromosome abnormalities, namely chromosome translocations and inversions, which are often associated with human hematopoietic tumors. It has been shown that the c-myc proto-oncogene is directly involved in the chromosome translocations t(8;14), t(2;8) and t(8;22) in Burkitt's lymphoma and that the c-abl proto-oncogene is activated through its fusion to the bcr gene as the result of the t(9;22) chromosome translocation in chronic myelogenous leukemia cells. The involvement of the immunoglobulin genes in chromosome translocations is very common in B-cell tumors, leading us to study the structure and function of the chromosome translocations in B-cell tumors. In this article, I describe the chromosome translocations associated with human B-cell tumors, focusing on how they occur, how they lead to cell transformation, and how new oncogenes involved in B-cell tumor development can be identified.
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  • Substances involved in cell differentiation of the cellular slime mold
    Dictyostelium discoideum
    Yohko YAMADA, Koji OKAMOTO
    1988 Volume 28 Issue 2 Pages 77-82
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.77
    JOURNAL FREE ACCESS
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    Quite a number of substances, such as cAMP, ammonia, DIF and others, are known to be involved in cell differentiation of the cellular slime mold. Some of them act as celltype specific inducers while others work as non-specific, general inducers.
    Their roles in cell differentiation are reviewed, including our results recently obtained.
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  • NADH-Ubiquinone Oxidoreductase
    Takao YAGI
    1988 Volume 28 Issue 2 Pages 83-86
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.83
    JOURNAL FREE ACCESS
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    The NADH-ubiquinone oxidoreductase of the mitochondrial respiratory chain catalyzes proton translocation across the inner membrane coupled to electron transfer. This is the largest enzyme complex in the mitochondrial oxidative phosphorylation system, and is composed of more than 25 unlike polypeptides. This article describes current knowledge of the enzyme and possible approaches to study of its structure and mechanisms of electron transfer and proton translocation.
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  • DNase I
    Michio SHIMOMURA
    1988 Volume 28 Issue 2 Pages 87-93
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.87
    JOURNAL FREE ACCESS
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    Investigations on purification, multiple forms, enzymic properties, functional amino acids, primary and tertiary structures of deoxyribonuclease I are briefly reviewed. The mechanism of DNase I action is going to be elucidated on the basis of chemical and physical studies.
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  • Bacteriorhodopsin as a Proton-Pumping Protein
    Akio MAEDA
    1988 Volume 28 Issue 2 Pages 94-98
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.94
    JOURNAL FREE ACCESS
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    Known facts on the interactions of the protonated Schiff base portion of the retinal chromophore of bacteriorhodopsin with the charge-carrying residues of the protein, and their changes in the light-induced intermediates were summarized and discussed in terms of a possible mechanism of the proton transport. Structural differences from halorhodopsin, a chloride pump, were also taken into considerations.
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  • Macroemulsion Science
    A Background for Understandings of the Dispersion State of Biological Components
    Sachio MATSUMOTO
    1988 Volume 28 Issue 2 Pages 99-102
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.99
    JOURNAL FREE ACCESS
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    This paper reviews briefly the works on dispersion state of a variety of macroemulsions and integrates advances made in the areas of colloid science so as to obtain futher insights into the formulation of non-equilibrium systems. The contents are divided into three sections: concept of macroemulsion state, type of emulsions in view of the phase diagram of mixed components, and formation of multiple emulsions.
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  • [title in Japanese]
    [in Japanese]
    1988 Volume 28 Issue 2 Pages 103-106
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.103
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    1988 Volume 28 Issue 2 Pages 107-109
    Published: March 25, 1988
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.28.107
    JOURNAL FREE ACCESS
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