Lysine residues of annexin VI are responsible for glycosaminoglycan- and phospholipid-binding activities
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概要
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Annexin VI is known to bind to glycosaminoglycans as well as phospholipids. We investigated the effects of chemical modification of annexin VI lysine residues on glycosaminoglycan-binding by solid phase assays and on phospholipid-binding by an optical biosensor system. As the concentration of the modifying reagent, pyridoxal 5'-phosphate, was increased, the extent of modification increased and the bindings of modified annexin VI to the ligands decreased, suggesting that lysine residues are important for the interactions of annexin VI with both glycosaminoglycans and phospholipids. Quantitatively however, the chemical modification affected the binding to glycosaminoglycans more than to phospholipids.
- お茶の水女子大学の論文
著者
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小島 京子
お茶の水大・理・化
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小島 京子
お茶の水女子大学理学部化学科
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Kimata Koji
Institute For Molecular Science Of Medicine Aichi Medical University
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Kojima Kyoko
Department Of Chemistry Faculty Of Science
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Kaneko K
Showa Univ. School Of Medicine Tokyo Jpn
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Matsumoto Isamu
Department Of Chemistry Faculty Of Science Ochanomizu University
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Ishitsuka R
Ochanomizu Univ. Tokyo Jpn
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Ishitsuka Reiko
Graduate School Of Humanities And Sciences Ochanomizu University
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Takagi Hidekazu
Institute For Molecular Science Of Medicine Aichi Medical University
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Kojima Kyoko
Department Of Chemistry Faculty Of Science Ochanomizu University
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Ishitsuka Reiko
Graduate School of Humanities and Sciences
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Matsumoto Isamu
Department of Chemistry, Faculty of Science, Ochanomizu University
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MATSUMOTO ISAMU
Department of Biochemistry, Kurume University School of Medicine
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