A silent beta-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 beta-X chain had a more anodic electrophoretic mobility; 38% of the total beta chain was of the abnormal type. Structural analysis using high-performance liquid chromatography and microsequencing procedures indicated a valine to isoleucine substitution at position beta 11(A8). This anomaly did not change the functional properties of the hemoglobin molecule. A mild reticulocytosis was observed in the propositus.
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Wong et al. (1984) studied this question.
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