Srouji A H, Macleod R M
Biochim Biophys Acta. 1976 Nov 26;453(1):15-25. doi: 10.1016/0005-2795(76)90246-4.
The corss-linking reagent p,p'-difluoro-m,m'-dinitrodiphenylsulfone has been used to fix in the tetramer form the various species of hemoglobin present in mixtures of hemoglobin A and hemoglobin C and of hemoglobin S and hemoglobin C. Following reaction, the presence of the hybrid hemoglobins alpha 2 A beta A beta C and alpha 2 A beta S beta C in these hemoglobin mixtures was demonstrated electrophoretically and the hybrids were isolated by ion-exchange chromatography. The identity of the alpha 2 A beta A beta C hybrid was further verified by peptide analysis. The success in cross-linking alpha 2 A beta 2 C, alpha 2 A beta A beta C, and alpha 2 A beta S beta C with p,p'-difluoro-m,m'-dinitrodiphenylsulfone shows that the distance between the alpha chain amino terminals in solution for these hemoglobin species is the same as in normal hemoglobin.
交联试剂对，对'-二氟-间，间'-二硝基二苯砜已被用于以四聚体形式固定血红蛋白A与血红蛋白C以及血红蛋白S与血红蛋白C的混合物中存在的各种血红蛋白种类。反应后，通过电泳证明了这些血红蛋白混合物中杂合血红蛋白α2AβAβC和α2AβSβC的存在，并通过离子交换色谱法分离出这些杂合体。通过肽分析进一步证实了α2AβAβC杂合体的同一性。用对，对'-二氟-间，间'-二硝基二苯砜成功交联α2Aβ2C、α2AβAβC和α2AβSβC表明，这些血红蛋白种类在溶液中α链氨基末端之间的距离与正常血红蛋白中的相同。
