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タイトル: | Effects of salts on the interaction of 8-anilinonaphthalene 1-sulphonate and thermolysin. |
著者: | Samukange, Vimbai Kamo, Masayuki Yasukawa, Kiyoshi Inouye, Kuniyo |
著者名の別形: | 井上, 國世 |
キーワード: | ANS metalloproteinase salt-induced activation salt-induced stabilization thermolysin |
発行日: | 9-Jun-2014 |
出版者: | Taylor & Francis Group |
誌名: | Bioscience, biotechnology, and biochemistry |
巻: | 78 |
号: | 9 |
開始ページ: | 1522 |
終了ページ: | 1528 |
抄録: | Neutral salts activate and stabilize thermolysin. In this study, to explore the mechanism, we analyzed the interaction of 8-anilinonaphthalene 1-sulphonate (ANS) and thermolysin by ANS fluorescence. At pH 7.5, the fluorescence of ANS increased and blue-shifted with increasing concentrations (0-2.0 μM) of thermolysin, indicating that the anilinonaphthalene group of ANS binds with thermolysin through hydrophobic interaction. ANS did not alter thermolysin activity. The dissociation constants (Kd) of the complex between ANS and thermolysin was 33 ± 2 μM at 0 M NaCl at pH 7.5, decreased with increasing NaCl concentrations, and reached 9 ± 3 μM at 4 M NaCl. The Kd values were not varied (31-34 μM) in a pH range of 5.5-8.5. This suggests that at high NaCl concentrations, Na(+) and/or Cl(-) ions bind with thermolysin and affect the binding of ANS with thermolysin. Our results also suggest that the activation and stabilization of thermolysin by NaCl are partially brought about by the binding of Na(+) and/or Cl(-) ions with thermolysin. |
著作権等: | The Version of Record of this manuscript has been published and is available inBioscience, Biotechnology, and Biochemistry (2014) http://www.tandfonline.com/ 10.1080/09168451.2014.923299. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 This is not the published version. Please cite only the published version. |
URI: | http://hdl.handle.net/2433/198454 |
DOI(出版社版): | 10.1080/09168451.2014.923299 |
PubMed ID: | 25209499 |
出現コレクション: | 学術雑誌掲載論文等 |
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