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Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Studies on the ferric derivatives.

ABSTRACT: The effect of inositol hexakisphosphate on the redox equilibria and on the c.d. spectra of ferric derivatives of haemoglobin from Camelus dromedarius has shown that: two distinct functionally relevant binding sites for polyanions are present on the protein; conformational changes promoted by inositol hexakisphosphate are largely dependent on spin state of the iron; tertiary and quaternary changes are not necessarily linked; structures induced by polyanions can be mixed forms that are neither T-state nor R-state.

SUBMITTER: Santucci R

PROVIDER: S-EPMC1146757 | biostudies-other | 1986 May

REPOSITORIES: biostudies-other

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Conformational changes induced by polyanions in haemoglobin from the dromedary (Camelus dromedarius). Role of chloride ions.

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Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Circular-dichroism study on the oxy derivative.

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Purification, crystallization and preliminary crystallographic study of haemoglobin from camel (Camelus dromedarius): a high oxygen-affinity lowland species.

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