Interaction between the synthesis of alpha and beta globin.

European Journal of Biochemistry
L M GarrickM D Garrick

Abstract

We have examined the relationship between alpha and beta globin chain syntheses by utilizing the distribution of isoleucyl residues in rabbit hemoglobin. The alpha globin chain contains three isoleucyl residues while the beta chain of certain rabbits contains no isoleucine. O-Methyl-L-threonine, an isoleucine isostere, inhibits incorporation of radiolabeled amino acids into alpha chains in rabbit reticulocytes. When alpha chain synthesis is inhibited by 50-85%, beta synthesis is stimulated by 15-50%. The excess labeled beta chains are not distinguishable from authentic beta chains by any of the following criteria: (a) carboxymethyl cellulose chromatography in sodium phosphate-urea buffers, (b) electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate, and (c) electrophoresis of methionine-containing tryptic peptides. The stimulation of beta synthesis continues after the pool of excess alpha chains has been exhausted by preincubation with O-methyl-L-threonine. The stimulation does not occur, however, when 1 mM 2-mercaptoethanol is added to the incubation medium or when the cells are excessively diluted in the incubation mixture. The rates of beta chain initiation and elongation during stimulation have been compare...Continue Reading

References

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Citations

Jul 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·R Y Walder, J A Walder
Mar 1, 1984·Journal of Cellular Physiology·D Binninger, L A Weber
Nov 1, 1977·European Journal of Biochemistry·A G StewartH R Arnstein
Sep 17, 1984·Biochemical and Biophysical Research Communications·M B Weinstein, H L Segal

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