Wong S C, Ali M A, Lam H, Webber B B, Wilson J B, Huisman T H
Am J Hematol. 1984 Jan;16(1):47-52. doi: 10.1002/ajh.2830160106.
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.