Biosynthesis of Hemoglobin Ann Arbor: Evidence for Catabolic and Feedback Regulation
J. G. Adams III 1,
W. P. Winter 1,
D. L. Rucknagel 1, and
H. H. Spencer 2
1 Department of Human Genetics, University of Michigan Medical School, Ann Arbor 48104
2 Veterans Administration Hospital, Ann Arbor, Michigan 48104
Hemoglobin Ann Arbor, in which arginine replaces leucine in position 80 of the a chain, occurs in aflected individuals in low proportion to hemoglobin A. Biosynthetic studies were perforined on reticulocytes of a patient heterozygous for this hemoglobin. These studies suggested that the low percentage of hemoglobin Ann Arbor is prinlarily due to preferential destruction of the abnormal component. The reduced concentration of
Ann Arbor chains was also reflected in a decreased synthesis of normal
chains.