Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 30 June 1972:
Vol. 176. no. 4042, pp. 1427 - 1429
DOI: 10.1126/science.176.4042.1427

Articles

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 agr Ann Arbor chains was also reflected in a decreased synthesis of normal beta chains.





To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)