Hemoglobin Hamilton or α2β211(a8)Val→Ile: A silent β-chain variant detected by triton X-100 acid-urea polyacrylamide gel electrophoresis

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Abstract
A silent β‐chain hemoglobin variant, not detectable by starch gel or agar gel electrophoresis was found using Triton X‐100 acid‐urea polyacrylamide gel electrophoresis. The abnormal β‐X chain had a more anodic electrophoretic mobility; 38% of the total β chain was of the abnormal type. Structural analysis using high‐performance liquid chromatography and microsequencing procedures indicated a valine to isoleucine substitution at position β11(A8). This anomaly did not change the functional proper ties of the hemoglobin molecule. A mild reticulocytosis was observed in the propositus.

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