Open AccessSolubilization of hemoglobin S by other hemoglobins.
Author(s) -
Ruth E. Benesch,
Rohinton Edalji,
Ruth E. Benesch,
Suzanna Kwong
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.9.5130
Subject(s) - hemoglobin , solubility , hemoglobin a , centrifugation , chemistry , hemoglobin a2 , polymerization , beta (programming language) , pellet , hemeprotein , alpha (finance) , biochemistry , chromatography , heme , polymer , biology , organic chemistry , enzyme , medicine , zoology , computer science , programming language , construct validity , nursing , patient satisfaction
The polymerization of mixtures of Hb S with hemoglobins A, A2, and F has been investigated by analysis of the proportions of S and non-S hemoglobin both in the supernate and in the pellet after centrifugation. In all cases the non-S hemoglobin was incorporated into the polymer even in the absence of hybrids in the order A > A2 > F. The solubility of Hb S is substantially increased by the other hemoglobins, especially by Hb F, which would account for its antisickling effect. It appears that the excluded volume effect of the other hemoglobin on Hb S is largely counterbalanced by the solubilizing effect arising from the interaction between the two hemoglobins in solution. The ability of hybrid hemoglobins to gel was demonstrated directly with tetramers in which alpha beta s dimers were covalently linked to alpha beta A, alpha delta A2, and alpha gamma F dimers.