Daha M R, Hazevoet H M, Vanes L A, Cats A
Immunology. 1980 Jul;40(3):417-24.
Sera from sixteen patients with SLE were investigated for the presence of a factor which would conserve convertase activity on preformed EAClgp 4hu2hu for 30 min at 30 degrees in EDTA. Although such a factor could not be detected readily in the sera, chromatography on DE-52 cellulose yielded fractions appearing as three peaks in one patient and as two peaks in a second patient. These peaks were capable of conserving C42 activity and were designated as F-42. Purification of F-42 from the second peak eluting between 4 and 7 mS on DE-52 was obtained by SP-C50, S-300 and QAE-A50 chromatography. F-42 exhibited charge heterogeneity upon SP-C50 chromatography. On polyacrylamide gel electrophoresis the final material migrated as one band, which coincided with the position of F-42 activity upon eluation from a parallel gel. F-42 had an apparent molecular weight of 150,000 and reacted with anti-IgG in Ouchterlony analysis. Sepharose-bound anti-IgG was capable of neutralizing F-42 activity. The purified material was shown to prolong the half-life (T 1/2) of performed cell-bound C42 in GVB-EDTA at 30 degrees from 5 to 80 min.
对16例系统性红斑狼疮（SLE）患者的血清进行检测，以寻找一种能在30℃的乙二胺四乙酸（EDTA）中，使预先形成的EAClgp 4hu2hu上的转化酶活性在30分钟内得以保留的因子。尽管在这些血清中未能轻易检测到这样一种因子，但在DE-52纤维素上进行层析时，在一名患者中得到的组分呈现为三个峰，在另一名患者中呈现为两个峰。这些峰能够保留C42活性，被命名为F-42。通过SP-C50、S-300和QAE-A50层析从DE-52上洗脱的第二个峰中纯化F-42。F-42在SP-C50层析时表现出电荷不均一性。在聚丙烯酰胺凝胶电泳中，最终产物迁移为一条带，这与从平行凝胶洗脱时F-42活性的位置一致。F-42的表观分子量为150,000，在双向免疫扩散分析中与抗IgG发生反应。琼脂糖结合的抗IgG能够中和F-42的活性。纯化后的物质显示，在30℃的GVB-EDTA中，能使预先形成的细胞结合C42的半衰期（T 1/2）从5分钟延长至80分钟。
