Role of gamma 87 Gln in the inhibition of hemoglobin S polymerization by hemoglobin F
نویسندگان
چکیده
منابع مشابه
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...
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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...
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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 ...
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Thiol reagents react with cysteine beta 93 of hemoglobin and as a result increase the oxygen affinity of hemoglobin. In the present studies we have used a thiol-disulfide exchange between mixed disulfides of hemoglobin and reduced glutathione to attach intracellular glutathione to hemoglobin and to study its antisickling properties. The rates of production of glutathionyl hemoglobin (G-Hb) depe...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)36918-1