Hemoglobin Ta-Li: β83 Gly→Cys
Journal
BBA - Protein Structure
Journal Volume
243
Journal Issue
3
Pages
467-474
Date Issued
1971
Author(s)
Abstract
Hb Ta-Li was discovered in 1970 in one male Chinese subject during our continuing survey for hemoglobin variants among Chinese school children. The subject was born in Ta-Li, Taiwan and was of Taiwanese (Fukienese) ancestry. The brother and mother of the subject also were found to have the Hb Ta-Li; all three are heterozygotes. Chemical structure studies have now established that the structural variation in Hb Ta-Li is located in the β chain at Position β-83 where a cysteinyl residue replaces the glycine group normally present at that location. In the propositus the relative amounts of Hb Ta-Li and Hb A0, as determined by column chromatographic separations, were 40:60, respectively. Hb Ta-Li is the second human hemoglobin variant known to involve the replacement of a normal constituent amino acid residue by a cysteinyl group. Previously Hb Pôrto Alegre, found in a Caucasian family in Brazil by other workers, was reported to be β9 Ser→Cys. In both variants the change occurs at a position on the outside molecular surface which allows polymerization of the molecule by disulfide bonding. In spite of this unusual property both Hb's Ta-Li and Pôrto Alegre appear to function normally and cause no noticeable anemia in the bearer. © 1971.
Type
journal article