Purification, molecular weight, and oxygen equilibrium of hemoglobin from Syngamus trachea, the poultry gapeworm

Hemoglobin from the parasitic nematode Syngamus trachea (Montagu, 1811) Chapin, 1925 (the poultry gapeworm) was purified on DEAE-cellulose at pH 9.0 using 0.01 to 0.1 M Tris-HCl buffer. This purified hemoglobin was electrophoretically homogeneous, and had a molecular weight of 38,400 as compared to 64,900 for hemoglobin from the host turkey, Meleagris gallopavo. The pressures of half saturation with oxygen of gapeworm hemoglobin are 10.2, 8.8, and 9.4 mm of Hg at pH values of 6.9, 7.1, and 7.5, respectively, as compared to 30.0, 24.1, and 22.5 mm of Hg for host hemoglobin at the same pH values. The gapeworm hemoglobin has less of a Bohr effect than the turkey hemoglobin.