Peptide Chain Synthesis of Human Hemoglobins A and A2

摘要: Abstract Human bone marrow was pulse-labeled with radioactive amino acids for various times. Hemoglobin A after 3 min of pulse showed a sudden increase in the relative specific activities peptides between position 90 and COOH terminus both α β chains. control point this region is postulated beyond which growth polypeptide chains markedly reduced, perhaps because assumption tertiary conformation growing heme insertion. Pulse labeling hemoglobin A2 indicates that δ are assembled at rate much less than either or A2. This can, part, account small quantity respect to found normal peripheral blood. Also, as cells age, their capacity produce lost greater A. The assembly hemoglobins proceeds about same rate, suggesting common pool two types synthesis cell.