Abstract
The effect of inositol hexakisphosphate (IHP) on the spectroscopic (EPR and absorbance) properties of the nitric oxide derivative of ferrous naturally glycated human hemoglobin HbA1c (HbA1cNO) has been investigated quantitatively. The results obtained show that 1) both in the absence and presence of IHP, the EPR and absorbance spectra of HbA1cNO show the same basic characteristics described for the nitrosyl derivative of ferrous HbA0, the nonglycated major component of human hemoglobin (HbA0NO); and 2) HbA1cNO binds IHP with an apparent dissociation equilibrium constant (θ{symbol} = 1.8 × 10-2 M), which is at least four orders of magnitude higher than that estimated for the polyphosphate interaction with HbA0NO (≤3 × 10-6 M). These data provide further independent evidence that interaction(s) of polyphosphates at the specific cleft between β-chains along the dyad-axis is sterically hindered in HbA1c by the presence of the two glucose residues covalently bound to the N-termini of β-chains, this finding being in agreement with the reduced effect of polyanions on HbA1c spectral and ligand-binding properties.
| Original language | English |
|---|---|
| Pages (from-to) | 19-24 |
| Number of pages | 6 |
| Journal | Journal of Inorganic Biochemistry |
| Volume | 34 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1988 |
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ASJC Scopus subject areas
- Biochemistry
- Inorganic Chemistry
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Effect of inositol hexakisphosphate on the spectroscopic properties of the nitric oxide derivative of ferrous naturally glycated human hemoglobin HbA1c . / Ascenzi, Paolo; Amiconi, Gino; Bertollini, Alberto; Coletta, Massimo; Brunori, Maurizio; Desideri, Alessandro; Bolognesi, Martino; Castagnola, Massimo.
In: Journal of Inorganic Biochemistry, Vol. 34, No. 1, 1988, p. 19-24.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Effect of inositol hexakisphosphate on the spectroscopic properties of the nitric oxide derivative of ferrous naturally glycated human hemoglobin HbA1c
AU - Ascenzi, Paolo
AU - Amiconi, Gino
AU - Bertollini, Alberto
AU - Coletta, Massimo
AU - Brunori, Maurizio
AU - Desideri, Alessandro
AU - Bolognesi, Martino
AU - Castagnola, Massimo
PY - 1988
Y1 - 1988
N2 - The effect of inositol hexakisphosphate (IHP) on the spectroscopic (EPR and absorbance) properties of the nitric oxide derivative of ferrous naturally glycated human hemoglobin HbA1c (HbA1cNO) has been investigated quantitatively. The results obtained show that 1) both in the absence and presence of IHP, the EPR and absorbance spectra of HbA1cNO show the same basic characteristics described for the nitrosyl derivative of ferrous HbA0, the nonglycated major component of human hemoglobin (HbA0NO); and 2) HbA1cNO binds IHP with an apparent dissociation equilibrium constant (θ{symbol} = 1.8 × 10-2 M), which is at least four orders of magnitude higher than that estimated for the polyphosphate interaction with HbA0NO (≤3 × 10-6 M). These data provide further independent evidence that interaction(s) of polyphosphates at the specific cleft between β-chains along the dyad-axis is sterically hindered in HbA1c by the presence of the two glucose residues covalently bound to the N-termini of β-chains, this finding being in agreement with the reduced effect of polyanions on HbA1c spectral and ligand-binding properties.
AB - The effect of inositol hexakisphosphate (IHP) on the spectroscopic (EPR and absorbance) properties of the nitric oxide derivative of ferrous naturally glycated human hemoglobin HbA1c (HbA1cNO) has been investigated quantitatively. The results obtained show that 1) both in the absence and presence of IHP, the EPR and absorbance spectra of HbA1cNO show the same basic characteristics described for the nitrosyl derivative of ferrous HbA0, the nonglycated major component of human hemoglobin (HbA0NO); and 2) HbA1cNO binds IHP with an apparent dissociation equilibrium constant (θ{symbol} = 1.8 × 10-2 M), which is at least four orders of magnitude higher than that estimated for the polyphosphate interaction with HbA0NO (≤3 × 10-6 M). These data provide further independent evidence that interaction(s) of polyphosphates at the specific cleft between β-chains along the dyad-axis is sterically hindered in HbA1c by the presence of the two glucose residues covalently bound to the N-termini of β-chains, this finding being in agreement with the reduced effect of polyanions on HbA1c spectral and ligand-binding properties.
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U2 - 10.1016/0162-0134(88)85014-1
DO - 10.1016/0162-0134(88)85014-1
M3 - Article
C2 - 2851030
AN - SCOPUS:0023789260
VL - 34
SP - 19
EP - 24
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 1
ER -