Lampe J, Pommerening K
Acta Biol Med Ger. 1975;34?710:1603-8.
Deoxyhemoglobin (deoxyHB) and oxyhemoglobin (HbO2) were covalently fixed to BrCN-activated Sephadex G-200. At pH 6, the oxygen semi-saturation pressure for the deoxyHb coupling product was 14.1, and for the HbO2 coupling product, 7.2 mm Hg. The alkaline Bohr effect delta was calculated to be - 0.55 and - 0.4 respectively. The Hill coefficients n are for both Hb derivatives between 1.4 and 1.5, independently of pH (for free Hb the respective values are pO2 50% = 18.2 mm Hg, delta = -0.55 and n = 2.5). Non-crosslinked dextran and Sephadex G-200 have no influence upon the affinity of free Hb to oxygen and upon cooperativity. As a reason for the varying oxygen-binding properties for the two Hb derivatives it is assumed that the amino group of valin alpha 1 is involved in the HbO2 fixation. In deoxyHb, this group is not probably converted. The reduced Hill coefficients and enhanced oxygen affinity are assumed to be due to impairment of the inter-chain contacts, to restrained cooperative mobility, and heterogeneity of the coupling products.
将脱氧血红蛋白（deoxyHB）和氧合血红蛋白（HbO2）共价固定在溴化氰活化的葡聚糖凝胶G - 200上。在pH 6时，脱氧血红蛋白偶联产物的氧半饱和压力为14.1，氧合血红蛋白偶联产物的氧半饱和压力为7.2毫米汞柱。计算得出碱性玻尔效应δ分别为 - 0.55和 - 0.4。两种血红蛋白衍生物的希尔系数n在1.4至1.5之间，与pH无关（游离血红蛋白的相应值为pO2 50% = 18.2毫米汞柱，δ = -0.55，n = 2.5）。非交联葡聚糖和葡聚糖凝胶G - 200对游离血红蛋白与氧的亲和力及协同性没有影响。对于两种血红蛋白衍生物不同的氧结合特性，推测缬氨酸α1的氨基参与了HbO2的固定。在脱氧血红蛋白中，该基团可能未发生转化。希尔系数降低和氧亲和力增强被认为是由于链间接触受损、协同运动受限以及偶联产物的异质性所致。
