Titlebook: Hemoglobin Disorders; Molecular Methods an Ronald L. Nagel Book 2003 Humana Press 2003

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Nucleation and Crystal Growth of Hemoglobins,ients expressing β.-globin (β6 Glu→Lys). In vitro, high-resolution structural determination by crystallographic methods requires the growth of Hb crystals to approx ∼1 mm in diameter, which may be induced by a variety of precipitants.

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Analysis of Hemoglobins and Globin Chains by High-Performance Liquid Chromatography,nique is used in two distinct approaches. The first is quantitative analysis of the various Hb fractions by ion-exchange HPLC, which is now done in routine hospital laboratories mostly by using fully automated systems. The second is reverse-phase (RP)-HPLC, which is of interest for more specialized

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Purification and Molecular Analysis of Hemoglobin by High-Performance Liquid Chromatograpy,HbA composes about 90% of the total Hb. It is made up of two identical α-chains and two identical β-chains. Besides HbA, human erythrocytes contain small amounts of other forms of Hb as fetal hemoglobin (HbF, α.γ.) and HbA. (α.δ.), and products of posttranslational modifications as HbA.. HbS, the si

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Oxygen Equilibrium Measurements of Human Red Blood Cells, are normal or not. If abnormal, there may be several reasons. One is an abnormality of the hemoglobin (Hb) itself. A second, more frequent reason, is a metabolic defect (or status) leading to change in the intraerythrocytic concentration of 2,3-diphosphoglycerate (DPG). Some toxic mechanisms may al

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Electrophoretic Methods for Study of Hemoglobins,mportant places in the history of the study of hemoglobin (Hb). HbS, the first abnormal Hb described, was discovered in 1949 by Pauling et al. (.), using moving boundary electrophoresis. Later, Hb variants were detected by zone electrophoresis on paper, starch gel, or cellulose acetate (.,.). With t

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