中文摘要：

目的：建立分离纯化血红蛋白α、β链方法。方法：对二氯汞苯甲酸（CPMB）处理的血红蛋白经CM SepharoseFF柱分离出结合有CPMB的α、β链，然后分别过Bio-gel p6柱除去α、β链上结合的CPMB。TricineSDS--PAGE检测蛋白分子量、纯度，采用琼脂糖弥散法监测抑茵效应。结果：该法成功分离出具较高纯度的血红蛋白α、β链，二者均具有杀大肠杆菌活性。结论：本分离程序简单、经济，可得到高纯度的天然a、B链，有助于对其后续的进一步研究。

英文摘要：

Objective： To establish a method for separating and purifying the alpha and beta subunits of human hemoglobin. Methotis： hemoglobin dealed with p-chloromercuribenzoate（CPMB）was applied to CM Sepharose FF column to get separated alpha-CPMB and beta-CPMB. Then CPMB was removed from alpha or beta chains by passing through Bio-gel p6 column respectively. The purified products were monitored by tricine SDS-PAGE. Agarose radial diffusion assay was used for their antimicrobial activity analysis. Results： High purity of alpha and beta chains were separated successfully, and the alpha and beta subunits of purified hemoglobin showed the activity against Escherichia coli. Conclusion： This isolation procedure was easy, economical and would be useful for the study of the multiple functions of hemoglobin and its frangments.