A New Assay Using Surface Plasmon Resonance (SPR) to Determine Binding of the Lactobacillus acidophilus Group to Human Colonic Mucin
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- UCHIDA Hideaki
- Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University
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- FUJITANI Kenji
- Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University
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- KAWAI Yasushi
- Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University
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- KITAZAWA Haruki
- Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University
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- HORII Akira
- Department of Molecular Pathology, Tohoku University School of Medicine
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- SHIIBA Kenichi
- Department of Gastrointestinal and Colorectal Surgery, Tohoku University School of Medicine
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- SAITO Kazuya
- Department of Gastrointestinal and Colorectal Surgery, Tohoku University School of Medicine
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- SAITO Tadao
- Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University
Bibliographic Information
- Other Title
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- New Assay Using Surface Plasmon Resonance SPR to Determine Binding of the Lactobacillus acidophilus Group to Human Colonic Mucin
- A New Assay Using Surface Plasmon Resonance (SPR) to Determine Binding of the<i>Lactobacillus acidophilus</i>Group to Human Colonic Mucin
- A new assay using surface plasmon resonance (SPR) to determine binding of the Lactobacillus acidophilius group to human colonic mucin
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Abstract
A new binding assay to investigate the mechanism of adhesion of lactic acid bacteria to the human intestine was established by the surface plasmon resonance technique using a biosensor BIACORE1000. Cells of 26 strains of the Lactobacillus acidophilus group as analytes were eluted onto a sensor chip on which were immobilized biotinylated A-trisaccharide polymer probes having human A-type antigen [(GalNAcα1-3(Fucα1-2)Gal)-] or human colonic mucin of blood type A (HCM-A) as ligands. In the first screening, high adhesive affinity to the A-trisaccharide BP-probe was observed in L. acidophilus OLL2769, L. crispatus JCM8778, LA205 and LA206. In the second screening, which used HCM-A, only L. acidophilus OLL2769 and L. crispatus JCM8778 were selected as adhesive strains with specific binding ability to human A-antigen. The results indicated that some strains of the L. acidophilus group could recognize and bind the sugar chain of A-antigen structure on HCM.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 68 (5), 1004-1010, 2004
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390001206473895424
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- NII Article ID
- 10013144409
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- NII Book ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD2cXkvVCgu7o%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 6957360
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- PubMed
- 15170102
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed