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

Abstract:

:The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopic (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.

journal_name

J Inorg Biochem

authors

Ascenzi P,Santucci R,Desideri A,Amiconi G

doi

10.1016/0162-0134(88)85001-3

subject

Has Abstract

pub_date

1988-04-01 00:00:00

pages

225-32

issue

4

eissn

0162-0134

issn

1873-3344

pii

0162-0134(88)85001-3

journal_volume

32

pub_type

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