Abstract
The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.
| Original language | English |
|---|---|
| Pages (from-to) | 225-232 |
| Number of pages | 8 |
| Journal | Journal of Inorganic Biochemistry |
| Volume | 32 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1988 |
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ASJC Scopus subject areas
- Biochemistry
- Inorganic Chemistry
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Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin. / Ascenzi, Paolo; Santucci, Roberto; Desideri, Alessandro; Amiconi, Gino.
In: Journal of Inorganic Biochemistry, Vol. 32, No. 4, 1988, p. 225-232.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin
AU - Ascenzi, Paolo
AU - Santucci, Roberto
AU - Desideri, Alessandro
AU - Amiconi, Gino
PY - 1988
Y1 - 1988
N2 - The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.
AB - The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.
UR - http://www.scopus.com/inward/record.url?scp=0023991998&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023991998&partnerID=8YFLogxK
U2 - 10.1016/0162-0134(88)85001-3
DO - 10.1016/0162-0134(88)85001-3
M3 - Article
C2 - 2454290
AN - SCOPUS:0023991998
VL - 32
SP - 225
EP - 232
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 4
ER -