Mechanical Instability of the Oxy-form of Sickle Haemoglobin

MUCH attention has been given to the molecular aspects of the deoxy form of sickle haemoglobin (Hb S) because sickling occurs with Hb S in the deoxygenated state. The oxy form of Hb S, on the other hand, is believed to be similar to normal adult haemoglobin (Hb A) with respect to solubility 1,2 , X-...

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Bibliographic Details
Published in:Nature (London) 1973-08, Vol.244 (5416), p.437-438
Main Authors: ASAKURA, T, AGARWAL, P. L, RELMAN, D. A, MCCRAY, J. A, CHANCE, B, SCHWARTZ, E, FRIEDMAN, S, LUBIN, B
Format: Article
Language:English
Subjects:
Hemoglobin, Sickle
Hemoglobins, Abnormal
Humanities and Social Sciences
Humans
Hydrogen-Ion Concentration
letter
multidisciplinary
Oxygen
Protein Denaturation
Science
Science (multidisciplinary)
Spectrophotometry
Temperature
Ultrasonics
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Summary:MUCH attention has been given to the molecular aspects of the deoxy form of sickle haemoglobin (Hb S) because sickling occurs with Hb S in the deoxygenated state. The oxy form of Hb S, on the other hand, is believed to be similar to normal adult haemoglobin (Hb A) with respect to solubility 1,2 , X-ray diffraction pattern 3 , oxygen binding 4 and other properties. During determination of oxygen equilibrium curves of Hb S, we noticed that a solution of oxyhaemoglobin S became turbid very easily when it was stirred or mixed. The turbidity was found to be due to protein which was denatured by the mechanical force involved and/or by foaming. Oxyhaemoglobin S denatured more quickly than oxyhaemoglobin A by mixing, stirring or sonication. The rate of denaturation was dependent on the oxygen concentration in the medium, suggesting that an oxidative process was involved. As demonstration of denaturation requires only a few drops of blood, water and shaking, this property can be used as a simple clinical test for the presence of Hb S.
ISSN:0028-0836
1476-4687
DOI:10.1038/244437a0