Abstract
Rat hemoglobins are unusually heterogeneous among mammals. This heterogeneity provides multiple opportunities for asynchronies in synthesis and degradation. We have examined rat hemoglobin turnover after an intravenous injection of 2-−14C-glycine. After analyzing incorporation into the seven nonallelic globin chains of adult rats, we found the percentage of the major β chain decreases over the red cell lifespan while the percentage of one of the minor β chains increases. This suggests that a post-synthetic mdification event converts a portion of the latter into the former.