Each of the electrophoretic components of human hemoglobin-haptoglobin 2-1 complexes designated in sequence from anode to cathode as Complex I, II, and III was isolated to elucidate the polymeric structures of human haptoglobin 2-1 proteins using preparative zone electrophoresis in acrylamide gel.
Combined with sedimentation and diffusion coefficients, the average molecular weights of Complex I, II, and III were estimated as 169, 000, 245, 000, and 342, 000, respectively. It is reasonable to conclude that Complex I will be a dimer of polymerizing unit of complex, (αβ)
Hb(αβ)
Hp2-1, Complex II a trimer, Complex III a tetramer, and therefore the polymer series of haptoglobin 2-1 proteins will be integral multiples of the monomeric Hp 2-1, (αβ)
Hp2-1.
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