Structure-Function Relations of Human Hemoglobins
نویسندگان
چکیده
منابع مشابه
Structure-function relations of human hemoglobins.
In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of smaller peptides, defined the molecular defect in HbS by showing that it differed from normal adult hemoglobin by only a single peptid...
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Cyclostomes, hagfishes and lampreys, contain hemoglobins that are monomeric when oxygenated and polymerize to dimers or tetramers when deoxygenated. The three major hemoglobin components (HbI, HbII, and HbIII) from the hagfish Myxine glutinosa have been characterized and compared with lamprey Petromyzon marinus HbV, whose x-ray crystal structure has been solved in the deoxygenated, dimeric stat...
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IFFERENCES IN THE HEMOGLOBINS of the adult and the newborn have been recognized since 1866 (36). Rapid advances in this field, however, began in 1949, when Pauling and Itano (25) discovered that the hemoglobin of sickle cell disease differs from adult hemoglobin. Since that time, 8 hemoglobins have been identified, hemoglobin C (18) in 1950, hemoglobin D (14) in 1951, hemoglobin E (7, 17) and h...
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The existence of two adult hemoglobin types, designated as hemoglobin A (or hemoglobin II) and hemoglobin B (or hemoglobin I), in various breeds of sheep is well established (for reference see van Vliet and Huisman (1)). The two molecular species have been separated both by electrophoresis, with which hemoglobin A showed the highest mobility at alkaline pH, and by chromatography on either Amber...
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ژورنال
عنوان ژورنال: Baylor University Medical Center Proceedings
سال: 2006
ISSN: 0899-8280,1525-3252
DOI: 10.1080/08998280.2006.11928171