Molecular size and subunit structure of the hemoglobins of Chironomus tentans.

The larval hemoglobins of the insect Chironomus fenfans, present in solution in hemolymph, were demonstrated to be exclusively monomeric with a molecular weight of approximately 15,900. This finding was based on studies of sedimentation velocity at various concentrations and with the use of agents generally effective in subunit separation, together with determinations by sedimentation equilibrium. No evidence of subunit aggregation was obtained. Column liltration studies suggest that the hemoglobins are more asymmetrical than myoglobin, but not to the extent of greatly altering sedimentation velocity. The monomeric nature of the molecule establishes a direct correspondence of hemoglobins to globin genes.