Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin

Paolo Ascenzi, Roberto Santucci, Alessandro Desideri, Gino Amiconi

Research output: Contribution to journalArticle

11 Citations (Scopus)

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 languageEnglish
Pages (from-to)225-232
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume32
Issue number4
DOIs
Publication statusPublished - 1988

Fingerprint

Camelus
Nitric Oxide
Hemoglobins
Derivatives
2,3-Diphosphoglycerate
Dextran Sulfate
Phytic Acid
Proteins
Dichroism
Protein Conformation
Paramagnetic resonance
Conformations
Heparin
Circular Dichroism
Binding Sites
polyanions

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

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 journalArticle

Ascenzi, Paolo ; Santucci, Roberto ; Desideri, Alessandro ; Amiconi, Gino. / Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin. In: Journal of Inorganic Biochemistry. 1988 ; Vol. 32, No. 4. pp. 225-232.
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AU - Amiconi, Gino

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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.

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