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.

Science 27 October 1967:
Vol. 158. no. 3800, pp. 488 - 490
DOI: 10.1126/science.158.3800.488
Prev | Table of Contents | Next

Articles

Rabbit Hemoglobin Biosynthesis: Use of Human Hemoglobin Chains To Study Molecule Completion

Joseph R. Shaeffer 1, Patricia K. Trostle 1, and Richard F. Evans 1

1 Department of Physics, M. D. Anderson Hospital and Tumor Institute, and University of Texas Graduate School of Biomedical Sciences, Houston 77025

A cell-free protein-synthesizing system made from rabbit reticulocytes was used to incorporate 14C-amino acids into hemoglobin. Electrophoretic analyses of the soluble products of this cell-free system revealed a fraction containing rabbit 14C-alpha chains in addition to the rabbit 14C-hemoglobin. The addition of isolated human hemoglobin beta chains to this system during active synthesis inhibited the release of newly synthesized rabbit 14C-beta chains into solution from the ribosome fraction. This inhibition was possibly a result of hybrid hemoglobin formation between rabbit alpha and human beta chains. A model of hemoglobin construction in which soluble alpha chains are intermediates is suggested. These alpha chains may aid in the release of beta chains from the polyribosomes during the completion of the hemoglobin molecule.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Translational Control in Hemoglobin Synthesis.
M. Rabinovitz, M. L. Freedman, J. M. Fisher, and C. R. Maxwell (1969)
Cold Spring Harb Symp Quant Biol 34, 567-578
   Abstract »    PDF »


To Advertise     Find Products

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