Identification of the adsorbing site of lysozyme onto the hydroxyapatite surface using hydrogen exchange and 1H NMR

FEBS Letters

Kawano, Keiichi¹  Terada, Yoshihiro¹  Nagadome, Hatsumi¹ 

[1] Faculty of Dentistry, Kyushu University 61, Maidashi 3-1-1, Higashi-ku, Fukuoka 812, Japan

关键词: Hydrogen exchange;    NMR;    Hydroxyapatite;    Lysozyme;    Adsorption;   

DOI  :  10.1016/0014-5793(93)81506-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The lysozyme-hydroxyapatite interaction was studied by measuring individual hydrogen-deuterium (H-D) exchange rates of amide protons. The H-D exchange reaction was initiated by transferring the lysozyme adsorbed on hydroxyapatite powder from H₂O into D₂O. After various H-D exchange time periods (pH 7.0, 25°C), the complex was dissociated and the remaining hydrogen label was determined by 2D NMR analysis. The H-D exchange rate of amide protons of residues 9, 11, 13, and 83 was slowed in the hydroxyapatite-lysozyme complex compared with free lysozyme. Residues 9, 11 and 13 positioned at the back of the active site would be the location of the binding site.

【 授权许可】

Unknown