Structural and binding properties of laminarin revealed by analytical ultracentrifugation and calorimetric analyses
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- 作者：Masayuki Odaa ; oda@kpu.ac.jp" class="auth_mail" title="E-mail the corresponding author ; Yoichi Tanabea ; Masanori Nodab ; Satomi Inabaa ; Elena Krayukhinab ; Harumi Fukadac ; Susumu Uchiyamab ; d
- 关键词：Analytical ultracentrifugation ; β-1 ; 3-glucan ; Carbohydrate-binding ; Differential scanning calorimetry ; Isothermal titration calorimetry
- 刊名：Carbohydrate Research
- 出版年：2016
- 出版时间：5 August 2016
- 年：2016
- 卷：431
- 期：Complete
- 页码：33-38
- 全文大小：844 K
文摘
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Laminarin mainly exists as a single-chain species.
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The binding thermodynamics of laminarin to glucanase could be determined.
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Analytical ultracentrifugation could detect the laminarin binding complex.