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Effect of amino acid at the b6 position on surface hydrophobicity, stability, solubility, and the kinetics of polymerization of hemoglobin. Comparisons among Hb A (Glub6), Hb C (Lysb6), Hb Machida (Glnb6), and Hb S (Valb6)



Effect of amino acid at the b6 position on surface hydrophobicity, stability, solubility, and the kinetics of polymerization of hemoglobin. Comparisons among Hb A (Glub6), Hb C (Lysb6), Hb Machida (Glnb6), and Hb S (Valb6)



The Journal of Biological Chemistry 262: 920-5




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Accession: 017870634

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Effect of amino acid at the beta 6 position on surface hydrophobicity, stability, solubility, and the kinetics of polymerization of hemoglobin. Comparisons among Hb A (Glu beta 6), Hb C (Lys beta 6), Hb Machida (Gln beta 6), and Hb S (Val beta 6). Journal of Biological Chemistry 262(27): 12920-5, 1987

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