Characterization of the changes in the state of aggregation induced by ligand binding in the hemoglobin system of a primitive vertebrate, the hagfish Eptatretus cirrhatus.

Hemoglobin (Hb) from the hagfish, Eptatretus cirrhatus, is composed of subunits of approx. 20,000 mol. wt. Aggregation of the deoxy subunits occurred, particularly at low pH and at high protein concentration. Oxygen equilibrium studies indicated slight cooperativity and the presence of a small, phosphate-independent Bohr effect. Equilibrium properties were protein concentration dependent indicating an oxygen-linked dissociation in the millimolar concentration range. Kinetic studies indicated a dimer to monomer transition in the micromolar concentration range. The ligand-binding character of hagfish Hb was similar to that of lampreys, but was governed by different kinetic and equilibrium parameters.