CAJ | 학술논문

目的综合再利用利凡诺去白蛋白人血浆进行抗凝血成分蛋白C（PC）和蛋白S（PS）的分离纯化。方法采用钡盐吸附、分段盐析、亲和层析和制备性等电聚焦等技术从利凡诺去白蛋白人血浆中分别纯化PC和PS。结果所得PC和PS的相对分子量分别为(61±0.9)、(83±0.8)kD；等电点分别为4.70±0.03、5.20±0.03；分别富含Glu、Leu、Gly 和Asp、Glu、Leu；毛细管区带电泳分析高度均一；与文献报道基本一致；得率分别为28.3%和12.6%。结论该纯化路线省时、经济，有助于利凡诺去白蛋白人血浆的综合再利用和抗凝血成分输血制剂的研制和开发。
목적종합재이용리범낙거백단백인혈장진행항응혈성분단백C（PC）화단백S（PS）적분리순화。방법채용패염흡부、분단염석、친화층석화제비성등전취초등기술종리범낙거백단백인혈장중분별순화PC화PS。결과소득PC화PS적상대분자량분별위(61±0.9)、(83±0.8)kD；등전점분별위4.70±0.03、5.20±0.03；분별부함Glu、Leu、Gly 화Asp、Glu、Leu；모세관구대전영분석고도균일；여문헌보도기본일치；득솔분별위28.3%화12.6%。결론해순화로선성시、경제，유조우리범낙거백단백인혈장적종합재이용화항응혈성분수혈제제적연제화개발。
Purpose　The aim is to isolate and purify Protein C(PC) and Protein S(PS) from no-albumin human plasma by rivanol precipitation. Methods　The isolated and purified steps included adsorption onto and elution from barium, salting-out, ion-exchange chromatography, affinity chromatography,preparative isoelectric focusing and so on. Results　The molecular weights of the obtained PC and PS were (61±0.9)kD and (83±0.8)kD, respectively, the isoelectric point, 4.70±0.03 and 5.20±0.03,and the yield, 28.3% and 12.6%. The purified PC and PS were shown to be highly homogeneous by capillary zone-electrophoresis(CZE), and rich in Glu, Leu and Gly or Asp, Glu and Leu respectively. Conclusion　 The methods could be used for large-scale isolation and purification of PC and PS from no-albumin human plasma.