Determination of ferric heme-human serum albumin by 1H NMR relaxometry

Mauro Fasano, Simona Baroni, Silvio Aime, Marco Mattu, Paolo Ascenzi

Research output: Contribution to journalArticlepeer-review


A new method for the accurate determination of ferric heme-human serum albumin (heme-HSA) at concentrations down to the physiological level, i.e., in the micromolar concentration range, is proposed. This method is based on the 1H NMR relaxometric properties of heme-HSA. Actually, the binding of the paramagnetic ferric heme to the primary binding site of HSA determines a strong paramagnetic enhancement of the water 1H NMR relaxation rate. Although a linear relationship may be seen by operating at 20 MHz on conventional electromagnets, the method here reported is improved by working at 0.02 MHz on a field-cycling instrument. This 1H NMR relaxometric method does not suffer from the presence in serum of heme catabolites (e.g., bilirubin) that affect significantly the optical determination of ferric heme-HSA in the micromolar concentration range. Paramagnetic ferric hemoglobin contribution may be selectively quenched by cyanide binding.

Original languageEnglish
Pages (from-to)64-67
Number of pages4
JournalJournal of Inorganic Biochemistry
Issue number1
Publication statusPublished - May 1 2003


  • H NMR relaxometry
  • Determination
  • Ferric heme-human serum albumin

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry


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