TY - JOUR
T1 - The effect of αthalassemia on the level of hybrid hemoglobin variants in heterozygotes
AU - Lanclos, K. D.
AU - Kutlar, A.
AU - Kutlar, F.
AU - Ojwang, P. J.
AU - Reese, A. L.
AU - Huisman, T. H.J.
N1 - Funding Information:
The authors are indebted to Drs. S . C . Wong, Montreal, Quebec, Canada, G.V. Sciarratta, Genova, Italy, and C. Romero Garcia, Madrid, Spain, for providing blood samples from Hb Lepore heterozygotes. This research was supported by USPHS Research Grants HLB-05168 and HLB-15158. This is contribution 110907 from the Department of Cell and Molecular Biology at the Medical College of Georgia in Augusta, Georgia.
PY - 1986
Y1 - 1986
N2 - The influence of a relative deficiency in α chain production on the amount of Hemoglobins Kenya, P-Nilotic, and Lepore was determined. The level of these hybrid hemoglobins in heterozygotes was correlated to various states of α chain deficiency by: 1) quantitation of the variants in blood samples and comparing these data with the number of α globin genes determined by gene mapping, 2) in vitro recombination experiments involving isolated non-α chains and normal α chains, and 3) in vitro heat stability analyses of the isolated hemoglobins. Hb Kenya, composed of normal α and γbeta; hybrid chains, is heat labile, has a decreased ability to combine with α chains, and its level in heterozygotes is greatly decreased when a concomitant αchain deficiency (αthalassemia) is present. Such a posttranslational control mechanism was not observed for Hb Lepore, with normal α chains and δbeta; hybrid chains, and Hb P-Nilotic, with normal α chains and βdelta; hybrid chains. The latter two variants are heat stable, and their hybrid chains combine equally well as normal β chains with normal α chains. Hb P-Nilotic is more heat stable than Hb A and its in vitro formation is increased over that of Hb S, and perhaps even Hb A, in conditions of severe α chain deficiency.
AB - The influence of a relative deficiency in α chain production on the amount of Hemoglobins Kenya, P-Nilotic, and Lepore was determined. The level of these hybrid hemoglobins in heterozygotes was correlated to various states of α chain deficiency by: 1) quantitation of the variants in blood samples and comparing these data with the number of α globin genes determined by gene mapping, 2) in vitro recombination experiments involving isolated non-α chains and normal α chains, and 3) in vitro heat stability analyses of the isolated hemoglobins. Hb Kenya, composed of normal α and γbeta; hybrid chains, is heat labile, has a decreased ability to combine with α chains, and its level in heterozygotes is greatly decreased when a concomitant αchain deficiency (αthalassemia) is present. Such a posttranslational control mechanism was not observed for Hb Lepore, with normal α chains and δbeta; hybrid chains, and Hb P-Nilotic, with normal α chains and βdelta; hybrid chains. The latter two variants are heat stable, and their hybrid chains combine equally well as normal β chains with normal α chains. Hb P-Nilotic is more heat stable than Hb A and its in vitro formation is increased over that of Hb S, and perhaps even Hb A, in conditions of severe α chain deficiency.
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U2 - 10.3109/03630268608996870
DO - 10.3109/03630268608996870
M3 - Article
C2 - 2427479
AN - SCOPUS:0022637932
SN - 0363-0269
VL - 10
SP - 401
EP - 416
JO - Hemoglobin
JF - Hemoglobin
IS - 4
ER -