MEMBRANE
Online ISSN : 1884-6440
Print ISSN : 0385-1036
ISSN-L : 0385-1036
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Volume 35, Issue 2
Displaying 1-8 of 8 articles from this issue
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Special Issue : Visualization of Membrane Structure and Function
Review Article
Original Contribution
  • Homology Modeling of an Algal Membrane Protein, Heterosigma Akashiwo Na+–ATPase
    Taeho Jo, Mariko Shono, Masato Wada, Sayaka Ito, Junko Nomoto, Yukichi ...
    2010 Volume 35 Issue 2 Pages 80-85
    Published: 2010
    Released on J-STAGE: June 14, 2015
    DOIhttps://doi.org/10.5360/membrane.35.80
    JOURNAL OPEN ACCESS
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    The three–dimensional structure of Heterosigma akashiwo Na+–ATPase (HANA) was predicted by means of homology modeling based on the crystal structure of the K+–bound form of shark Na+/K+–ATPase (PDB ID: 2ZXE). The overall structure of HANA appears to be similar to that of shark Na+/K+–ATPase. Both contain three characteristic cytoplasmic domains, A, N and P, which are unique to P–type ATPases. HANA has a long TM7–8 junction as a large extracellular domain, in place of the β–subunit of shark Na+/K+–ATPase. Two putative K+–binding sites in the transmembrane domain of HANA were identified by means of valence mapping based on the constructed structure. The presence of K+–binding sites and the reported ion requirements for ATPase activity and EP formation indicate that HANA may transport K+ ions in the same manner as animal Na+/K+–ATPases.
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  • Carboxybetaine–Group Immobilized onto Pore Surface Reduced Protein Adsorption to Porous Membrane
    Shinya Matsuno, Akio Iwanade, Daisuke Umeno, Kyoichi Saito, Hajime Ito ...
    2010 Volume 35 Issue 2 Pages 86-92
    Published: 2010
    Released on J-STAGE: June 14, 2015
    DOIhttps://doi.org/10.5360/membrane.35.86
    JOURNAL OPEN ACCESS
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    N, N–dimethyl–γ–aminobutyric acid (DMGABA) as a carboxybetaine was introduced into the polymer chain grafted onto the pore surface of a polyethylene-made porous hollow-fiber membrane. The DMGABA–immobilized porous hollow-fiber membrane (DMGABA fiber) was prepared by the radiation–induced graft polymerization of glycidyl methacrylate (GMA) and the subsequent addition of DMGABA to the epoxy group of the grafted poly–GMA chain. The dose of the electron beam, the degree of GMA grafting (dg), and the molar conversion of the epoxy group into the DMGABA group were optimized to minimize the amount of protein adsorbed. As a result, a dose of 200 kGy, a dg of 140%, and a molar conversion above 3% were selected from the viewpoints of the protein binding capacity of the DMGABA fiber. The binding capacity of the DMGABA fiber for lysozyme in carbonate buffer (pH 9.0) was reduced to less than 10% that of the original polyethylene membrane. The lysozyme binding capacity of the DMGABA fiber in Britton–Robinson universal buffer (pH 7.0) was 17 ng per cm2 of the pore surface.
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