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

ABSTRACT: The c.d. spectrum of oxyhaemoglobin from Camelus dromedarius is significantly affected by the presence of inositol hexakisphosphate. Correlation with O2-binding measurements shows that these dichroic changes parallel the functional properties of the protein. The optical modifications suggest that, in contrast with human haemoglobin, the conformational changes induced by inositol hexakisphosphate on dromedary oxyhaemoglobin are mainly attributable to a local change of the tertiary structure reminiscent of that of the deoxy derivative, the quaternary conformation seeming to be almost unaffected. The results provide direct evidence of the existence on the protein of two distinct sites for polyanions.

SUBMITTER: Santucci R

PROVIDER: S-EPMC1152821 | biostudies-other | 1985 Nov

REPOSITORIES: biostudies-other

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

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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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Tuberculosis caused by Mycobacterium caprae in a camel (Camelus dromedarius).

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