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

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Abstract
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.

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