Chiu W Y, Yamada K, Saito A, Ogawa H, Takagi T, Chung T G
Nagoya University Branch Hospital, Japan.
J Chromatogr. 1988 Jun 24;428(1):25-33. doi: 10.1016/s0378-4347(00)83887-6.
Partly protein-permeable haemodialysers were evaluated during haemodialysis therapy for removal of serum low-molecular-mass proteins (10,000-76,000) in patients with chronic renal failure. The six haemodialyser membranes used were cuproammonium rayon (CL-S12W), cellulose acetate (Duo-Flux HP and FF-22), ethylene-vinyl alcohol copolymer (KF-101-15), polyacrylonitrile (H12-2400S) and polymethyl methacrylate (BK2.0H). The analysis was carried out by gel permeation chromatography, sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis (2-DE). The removal of ten serum proteins per haemodialysis therapy was also carried out by the immunodiffusion method. The protein removal in each haemodialyser is qualitatively comparable to that obtained by SDS-PAGE and 2-DE. beta 2-Microglobulin in the haemodialysate obtained with BK2.0H was removed to a lesser extent than that from the other haemodialysers, which seems to be the reason for its adsorption in the BK2.0H haemodialyser, which contains a polymethyl methacrylate membrane. The amount of serum protein excretion during haemodiafiltration treatment using the partly protein-permeable haemodialysers decreased in the order KF-101-15C greater than BK2.0H greater than CL-S12W greater than Duo-Flux HP greater than FF-22 greater than H12-2400S.
在慢性肾衰竭患者的血液透析治疗过程中,对部分蛋白质可通透的血液透析器进行了评估,以测定其对血清低分子量蛋白质(10,000 - 76,000)的清除能力。所使用的六种血液透析器膜分别为铜氨人造丝(CL - S12W)、醋酸纤维素(Duo - Flux HP和FF - 22)、乙烯 - 乙烯醇共聚物(KF - 101 - 15)、聚丙烯腈(H12 - 2400S)和聚甲基丙烯酸甲酯(BK2.0H)。分析通过凝胶渗透色谱法、十二烷基硫酸钠聚丙烯酰胺凝胶电泳(SDS - PAGE)和二维凝胶电泳(2 - DE)进行。每次血液透析治疗对十种血清蛋白质的清除情况也通过免疫扩散法进行测定。每种血液透析器对蛋白质的清除在定性上与通过SDS - PAGE和2 - DE获得的结果相当。用BK2.0H获得的透析液中β2 - 微球蛋白的清除程度低于其他血液透析器,这似乎是其在含有聚甲基丙烯酸甲酯膜的BK2.0H血液透析器中吸附的原因。使用部分蛋白质可通透的血液透析器进行血液透析滤过治疗期间,血清蛋白排泄量按以下顺序降低:KF - 101 - 15C>BK2.0H>CL - S12W>Duo - Flux HP>FF - 22>H12 - 2400S。