The structural alterations induced by covalent binding as well as by adsorption of aquomethaemoglobin (Hb) to Sephadex matrices are investigated by proton magnetic relaxation. It is shown that the quaternary structure and inositol hexaphosphate binding ability are preserved in covalently bound Hb. Here the haem pockets in a chains tighten, while adsorption increases the dynamics of solvent protons in the haem pockets, probably due to their loosening. It is concluded that the structure of an immobilized protein is dependent on the type of binding.
|Original language||English (US)|
|Number of pages||5|
|State||Published - Jan 1 1976|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)