Amiconi G, Zolla L, Vecchini P, Brunori M, Antonini E
Eur J Biochem. 1977 Jun 15;76(2):339-43. doi: 10.1111/j.1432-1033.1977.tb11601.x.
The binding of dextran sulphate and heparin to human hemoglobin and their effect on the properties of gas transport have been investigated. Both dextran sulphate and heparin are strongly bound by oxy-hemoglobin as well as deoxyhemoglobin and the stoichiometry of the binding (polyanion/tetrameric hemoglobin) is less than unity; sedimentation analysis gives indication for the existence of octomers. The oxygen affinity of hemoglobin is decreased, to the same extent, by both dextran sulphate and heparin. This effect is pH-dependent. In addition the polyanions affect the position and the magnitude of the Bohr effect. In the presence of dextran sulphate the recombination of hemoglobin with carbon monoxide after flash photolysis is biphasic and the fraction of quickly reacting material increases with dilution of the protein.
研究了硫酸葡聚糖和肝素与人血红蛋白的结合及其对气体运输特性的影响。硫酸葡聚糖和肝素都能与氧合血红蛋白以及脱氧血红蛋白紧密结合，且结合的化学计量比（聚阴离子/四聚体血红蛋白）小于1；沉降分析表明存在八聚体。硫酸葡聚糖和肝素都能使血红蛋白的氧亲和力降低相同程度。这种效应依赖于pH值。此外，聚阴离子会影响玻尔效应的位置和大小。在硫酸葡聚糖存在下，闪光光解后血红蛋白与一氧化碳的重组是双相的，快速反应物质的比例随蛋白质稀释而增加。
