![Sample our Medicine, Dentistry, Nursing & Allied Health journals, sign in here to start your FREE access for 14 days]({"type":"image" , "src" : "/sda/5944/TOC-Subject-Sample-2021-Medicine-Dentistry-Nursing-Allied-Health.jpg"})
Abstract
In 1973 Asakura demonstrated that, following mechanical shaking, oxy-Hb S was much less stable than oxy-Hb A (Nature 244: 437, 1973). We have studied the mechanical stability of Hb Créteil (β89 Ser→Asn), Hb Hope (β136 Gly→Asp), Hb Strasbourg (β23 Val→Asp), and the hybrid Hb S/Stanleyville-II (β6 Glu→Val; α78 Asn→Lys) by the method of Roth et al. (Blood 45:377, 1975). Hb Créteil, Hb Hope, and Hb S/St-II were sensitive to mechanical shaking, while Hb Strasbourg was more stable than Hb A, a hitherto undescribed finding.
The precise mechanisms responsible for this precipitation are not known. From comparisons with published results, but excluding thermosensitive Hbs, we conclude that:
—standard methods for isolation of hemoglobins modify its mechanical stability
—alpha mutation increases the mechanical stability of Hb S in the hybrid Hb S/St-II
—some mutations produce a more stable hemoglobin than Hb A.