Sparing effect of hemoglobin F and hemoglobin A2 on the polymerization of hemoglobin S at physiologic ligand saturations.

Sparing effect of hemoglobin F and hemoglobin A2 on the polymerization of hemoglobin S at physiologic ligand saturations.

Recent interest in therapies for sickle cell anemia based on elevating fetal Hb has made accurate estimates of the sparing effect of fetal Hb (Hb F) and other non-sickle Hbs on sickle Hb (Hb S) polymerization essential. We have developed a technique, using HbCO as surrogate for HbO2, that enables us to assess the solubility of Hb S as a function of ligand saturation under conditions that mimic ...

Polymerization of Recombinant Hemoglobin F yE6V and Hemoglobin F yE6V, yQ87T Alone, and in Mixtures With Hemoglobin S

To further understand determinants for Hemoglobin (Hb) S polymerization, as well as the inhibitory mechanism of Hb F on Hb S polymerization, Hb F variants containing Val-* (Hb F yE6V) or Val-*, Thr-y87 (Hb F yE6V. yQ87Tj were expressed in yeast. The oxy form of Hb F yE6V was about 10-fold less stable to mechanical agitation than native oxy Hb F, which is similar to stability differences compari...

Studies on Hemoglobin Biosynthesis: Asynchronous Synthesis of Hemoglobin a and Hemoglobin A2 by Erythrocyte Precursors.

Influence of hemoglobin S adducts on hemoglobin A2 quantification by HPLC.

Role of $ 37 Gln in the Inhibition of Hemoglobin S Polymerization by Hemoglobin

Previous studies suggested that y87 Gln in hemoglobin (Hb) F is an important site for promoting inhibition of Hb S (cy#: polymerization by H b F. We engineered and isolated the double mutant ) using a yeast expression system and characterized polymerization properties of this modified tetramer in an effort to clarify the role of Gln at position 87 in inhibiting H b S polymerization. Electrop...