期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1970
卷号：65
期号：3
页码：697-701
DOI：10.1073/pnas.65.3.697
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Mutant, unstable hemoglobins precipitate as Heinz bodies in circulating red blood cells resulting in their premature hemolysis. We stress that generally these hemoglobins contain amino acid substitutions in the {beta}-chain of globin near the heme pocket, and demonstrate that heme binding suffers thereby. Four genetically unstable hemoglobins lost roughly half their heme content while precipitating into Heinz bodies. Conversely, repletion of hemes in vitro corrected the characteristically aberrant electrophoretic mobilities of these hemoglobins and concomitantly prevented their excessive denaturation into Heinz bodies. From the finding that heme-containing [α]-chains accumulate in solution during Heinz body formation, we propose that heme loss occurs predominantly from mutant {beta}-chains, which then precipitate. This mechanism of Heinz body formation is valid in most, but not all, the unstable hemoglobinopathies.
