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Determination of ferric heme-human serum albumin by 1H NMR relaxometry
- Publication Year :
- 2003
- Publisher :
- Elsevier Science Incorporated / NY Journals:Madison Square Station, PO Box 882:New York, NY 10159:(212)633-3730, EMAIL: usinfo-f@elsevier.com, INTERNET: http://www.elsevier.com, Fax: (212)633-3680, 2003.
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Abstract
- 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 1 H 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 1 H 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 1 H 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.
- Subjects :
- Relaxometry
biology
Chemistry
Cyanide
Inorganic chemistry
Serum albumin
Heme
Human serum albumin
Biochemistry
Inorganic Chemistry
chemistry.chemical_compound
medicine
Proton NMR
biology.protein
Ferric
Humans
Hemoglobin
Nuclear Magnetic Resonance, Biomolecular
Serum Albumin
medicine.drug
Protein Binding
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....c087324ae66f048307a2236e611640e6