Home LiteratureArticle Details
PMID: 5033650 Published · ppublish English Journal Article

Biosynthesis of hemoglobin Ann Arbor: evidence for catabolic and feedback regulation.

Science (New York, N.Y.) ·Vol. 176 ·No. 4042 ·1972-06-30 ·Pages 1427-9

Adams JG, Winter WP, Rucknagel DL, Spencer HH

Abstract

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

MeSH Terms
Amino Acids/analysis,metabolism Anemia, Hemolytic/metabolism Autoradiography Carbon Isotopes Chromatography Chromatography, Gel Hemoglobinopathies/metabolism Hemoglobins, Abnormal/analysis,biosynthesis Humans Male Reticulocytes/metabolism Tritium
Chemicals
Amino Acids Carbon Isotopes Hemoglobins, Abnormal Tritium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Adams J G
Winter W P
Rucknagel D L
Spencer H H
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1972-06-30
Pages
1427-9
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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