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- W2048768478 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." @default.
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- W2048768478 date "1981-01-01" @default.
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- W2048768478 title "Effect of Some physical Features and of Amino acid Substitutions on the Mechanical Precipitation of Hemoglobin" @default.
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- W2048768478 doi "https://doi.org/10.3109/03630268108991812" @default.
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