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 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 language | English |
|---|---|
| Pages (from-to) | 64-67 |
| Number of pages | 4 |
| Journal | Journal of Inorganic Biochemistry |
| Volume | 95 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - May 1 2003 |
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Keywords
- H NMR relaxometry
- Determination
- Ferric heme-human serum albumin
ASJC Scopus subject areas
- Biochemistry
- Inorganic Chemistry
Cite this
Determination of ferric heme-human serum albumin by 1H NMR relaxometry. / Fasano, Mauro; Baroni, Simona; Aime, Silvio; Mattu, Marco; Ascenzi, Paolo.
In: Journal of Inorganic Biochemistry, Vol. 95, No. 1, 01.05.2003, p. 64-67.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Determination of ferric heme-human serum albumin by 1H NMR relaxometry
AU - Fasano, Mauro
AU - Baroni, Simona
AU - Aime, Silvio
AU - Mattu, Marco
AU - Ascenzi, Paolo
PY - 2003/5/1
Y1 - 2003/5/1
N2 - 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.
AB - 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.
KW - H NMR relaxometry
KW - Determination
KW - Ferric heme-human serum albumin
UR - http://www.scopus.com/inward/record.url?scp=0037405541&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037405541&partnerID=8YFLogxK
U2 - 10.1016/S0162-0134(03)00070-9
DO - 10.1016/S0162-0134(03)00070-9
M3 - Article
C2 - 12706543
AN - SCOPUS:0037405541
VL - 95
SP - 64
EP - 67
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 1
ER -