The gelation of deoxyhemoglobin S in erythrocytes as detected by transverse water proton relazation measurements |
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Authors: | G L Cottam K M Valentine K Yamaoka M R Waterman |
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Institution: | Department of Biochemistry, The University of Texas Southwestern Medical School at Dallas, Dallas, Texas 75235 USA |
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Abstract: | At 37 °C, when samples of blood, washed erythrocytes, or isolated hemoglobin from individuals with sickle cell disease are deoxygenated, the transverse water proton relaxation time is sharply decreased. In similar samples from normal adults homozygous for hemoglobin A, only a slight decrease in t2 is observed upon deoxygenation at 37 °C. In samples containing deoxyhemoglobin S the value of t2 increases as the temperature is decreased from 37 °C to 4 °C, in contrast to samples containing oxyhemoglobin S, oxyhemoglobin A, or deoxyhemoglobin A where t2 decreases as the temperature decreases. It is suggested that this decrease in t2 observed in samples of deoxyhemoglobin S at 37 °C is the result of an increase in the amount of preferentially oriented water at macromolecular interfaces which occurs under conditions known to produce deoxyhemoglobin S gelation. Conditions which reverse deoxyhemoglobin S gelation such as lowering the temperature to 4 °C decrease the amount of preferentially oriented water which results in an increase in the value of t2. Thus, measurement of the transverse water proton relaxation time can be used to monitor the gelation of deoxyhemoglobin S inside the erythrocyte. |
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