Matrix bound haemoglobin as seen by proton magnetic relaxation

B. Benko, S. Vuk Pavlovic, K. Pommerening

Research output: Contribution to journalArticlepeer-review


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 languageEnglish (US)
Pages (from-to)157-161
Number of pages5
JournalStudia Biophysica
Issue number3
StatePublished - 1976

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology
  • Biophysics


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