Hemoglobin Hamilton or α<sub>2</sub>β<sub>2</sub>11(a8)Val→Ile: A silent β‐chain variant detected by triton X‐100 acid‐urea polyacrylamide gel electrophoresis

AbstractA 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.

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