Baumann, Rosemarie and Goetz, Robert and Dragon, Stefanie (2003) NTP pattern of avian embryonic red cells: role of RNA degradation and AMP deaminase/5 '-nucleotidase activity. AMERICAN JOURNAL OF PHYSIOLOGY-REGULATORY INTEGRATIVE AND COMPARATIVE PHYSIOLOGY, 284 (3). R771-R779. ISSN 0363-6119
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During terminal erythroid differentiation, degradation of RNA is a potential source for nucleotide triphosphates (NTPs) that act as allosteric effectors of hemoglobin. In this investigation, we assessed the developmental profile of RNA and purine/pyrimidine trinucleotides in circulating embryonic chick red blood cells (RBC). Extensive changes of the NTP pattern are observed which differ significantly from what is observed for adult RBC. The biochemical mechanisms have not been identified yet. Therefore, we studied the role of AMP deaminase and IMP/GMP 5'-nucleotidase, which are key enzymes for the regulation of the purine nucleotide pool. Finally, we tested the effect of major NTPs on the oxygen affinity of embryonic/adult hemoglobin. The results are as follows. 1) Together with ATP, UTP and CTP serve as allosteric effectors of hemoglobin. 2) Degradation of erythroid RNA is apparently a major source for NTPs. 3) Developmental changes of nucleotide content depend on the activities of key enzymes (AMP deaminase, IMP/GMP 5'-nucleotidase, and pyrimidine 5'-nucleotidase). 4) Oxygen-dependent hormonal regulation of AMP deaminase adjusts the red cell ATP concentration and therefore the hemoglobin oxygen affinity.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HUMAN-ERYTHROCYTES; DEAMINASE ACTIVITY; ADENOSINE-DEAMINASE; OXYGEN-AFFINITY; CHICKEN EMBRYOS; BLOOD-CELLS; 5'-NUCLEOTIDASE; PURIFICATION; HEMOGLOBIN; CATABOLISM; nucleotide triphosphates; hemoglobin; oxygen affinity |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Physiologie > Alumni or Retired > Prof. Dr. Rosemarie Baumann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 15 Sep 2021 10:17 |
| Last Modified: | 15 Sep 2021 10:17 |
| URI: | https://pred.uni-regensburg.de/id/eprint/39212 |
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