engleski

The Matrix-Bound Haemoglobin as seen by Proton Magnetic Relaxation

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.

Adsorption; Haemoglobin; Sephadex; Proton magnetic relaxation

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