PMID: 1138906May 1, 1975

Biogenesis of erythrocyte membrane proteins. In vivo studies in anemic rabbits

Biochimica Et Biophysica Acta
P A KochJ R Carter

Abstract

To study the process of red cell membrane protein synthesis we have followed the time course of [3-H]leucine appearance in total protein and individual peptides of the erythrocyte membrane following injection of the amino acid into phenylhydrazine-anemic rabbits. Multiple peripheral blood samples were taken from single animals over a 5-week period. Erythrocyte membrane proteins were separated by polyacrylamide gel electrophoresis in sodium dodecylsulfate and dithiothreitol; incorporation of radioactivity was determined by gel slicing and liquid scintillation spectrometry. Appearance of [3-H]leucine in circulating erythrocytes reached a peak at 1-3 days, with a steady decline thereafter. The radioactive amino acid appeared first in the lowest molecular weight peptides and last in the largest peptides; at the earliest time point (8 h), little radioactivity was observed in any of the four largest peptides present in the membranes (bands A, 1, 2 and 3). Certain smaller peptides (bands 4, 5 and 9) were the predominant species labeled at this time. By 24 h all peptides showed significant incorporation. With maturation of the red cells, label largely disappeared from bands A, 9 and several smaller peptides; this was confirmed by findi...Continue Reading

References

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Citations

Jan 1, 1982·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·R J HowardG F Mitchell
Sep 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·H ChangH F Lodish
Aug 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·A M Weigensberg, R Blostein
Sep 1, 1987·The Journal of Cell Biology·M Hanspal, J Palek
Feb 1, 1981·British Journal of Haematology·S H KrasnowS K Ballas
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Related Concepts

Anemia
Serum Proteins
Plasma Membrane
Erythrocytes
Eryhem
Leucine
Polypeptides
Phenylhydrazines
Reticulocytes

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