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  • Title: Hemoglobin Tampa:beta 79 (EF3) aspartic acid replaced by tyrosine.
    Author: Johnson MH, Jue DL, Patchen LC, Hartwig EC, Schneider NJ, Moo-Penn WF.
    Journal: Biochim Biophys Acta; 1980 May 29; 623(1):119-23. PubMed ID: 7378467.
    Abstract:
    Hemoglobin Tampa was detected in a 6-year-old male caucasian who is homozygous for this variant hemoglobin. The variant hemoglobin has an electrophoretic mobility between Hb F and Hb S on cellulose acetate (pH 8.5) and a mobility between Hb S and Hb C on citrate agar (pH 6.0). In acid buffer globin chain analysis revealed an abnormal beta chain with a mobility between the beta A and beta S chains, and in alkaline buffer the mobility of the chain was at the beta S position. Structural characterization of the variant beta chain indicates that aspartic acid is replaced with tyrosine at position 79, the site of a previously reported mutation, Asp replaced by Gly (Hb Hsi-Tsou). The clinical histories of the available family members including the homozygous propositus appear to be unremarkable.
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