[Incidence of abnormal hemoglobins in Venezuelan children].
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An electrophoretically slowly moving hemoglobin variant, Hb Yusa, was found in a 48-year-old man, his younger sister and mother. No clinical or hematological abnormalities were seen in the individuals heterozygous for this mutant gene. Structural studies of this abnormal hemoglobin showed a new type substitution of beta 21 (B3) Asp leads to Tyr. The percentage of the abnormal hemoglobin in the hemolysate was 40.8. The hemoglobin had neither instability nor functional abnormality.
Hemoglobins H and Bart's failed to bind human haptoglobin. The binding of hemoglobins A(1), F, I, and Lepore was comparable to that of hemoglobin A. These findings suggest that configurational differences or the absence of alpha chain dimers was responsible for the lack of binding of hemoglobins H and Bart's.
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