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Identification of the adsorbing site of lysozyme onto the hydroxyapatite surface using hydrogen exchange and 1 H NMR
Author(s) -
Nagadome Hatsumi,
Kawano Keiichi,
Terada Yoshihiro
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81506-u
Subject(s) - lysozyme , chemistry , adsorption , identification (biology) , hydrogen , nuclear chemistry , chromatography , chemical engineering , inorganic chemistry , biochemistry , organic chemistry , biology , botany , engineering
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 H 2 O into D 2 O. 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.