Functional Properties of Hemoglobin Kempsey
نویسندگان
چکیده
منابع مشابه
Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, hemoglobin Kempsey.
\TO CLASSES of amino acid substitutions in hemoglobins have profound effects on the major function of this protein, oxygen transport. The first includes the hemoglobins M’ and hemoglobin Kansas,2 which result in cyanoSis in heterozygous subjects and no significant erythrocytosis. The second class, represented by hemoglobin Chesapeake3 and hemoglobin Yakima,4 is assocated with erythrocytosis in ...
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Hemoglobin Bethesda is a /3 chain variant of human hemoglobin in which histidine is substituted for tyrosine at position 145. From chemical and crystallographic studies, it has been postulated that the tyrosine normally found at this position is critical for the maintaince of a normal deoxy structure. Kinetic studies of the carbon monoxide and Rbutyl isocyanide binding reactions show that deoxy...
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Hemoglobins (Hb) Yakima and Kempsey were purified from patients' blood with diethylaminoethyl cellulose column chromatography. The oxygen equilibrium curves of the two hemoglobins and the effects of organic phosphates on the function were investigated. In 0.1 M phosphate buffer, Hill's constants n for Hb Yakima and Hb Kempsey were 1.0 to 1.1 at the pH range for 6.5 to 8.0 and the oxygen affinit...
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Blood and stripped hemoglobin from Nelore cattle individuals were submitted to oxygen equilibrium experiments in both gasometric and spectrophotometric methods. No difference was detected in oxygen affinity and Bohr effect among Hb A, Hb B and Hb AB in experiments with both blood and stripped hemoglobin, in the presence and absence of the chloride ion. However, n values (Hill plots) were higher...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)81254-1