Norton P A, Slayter H S
Proc Natl Acad Sci U S A. 1981 Mar;78(3):1661-5. doi: 10.1073/pnas.78.3.1661.
Human fibrinogen was digested with trypsin to yield core fragments D and E, and antibodies were made against the isolated fragments. The Fab' fragments derived from these antibodies were mixed with native fibrinogen, resulting in the formation of soluble immune complexes. These were rotary shadowed with platinum or negatively contrasted with uranyl acetate and examined by electron microscopy. Fab' from anti-D immunoglobulin was found to be attached to the outer nodules of fibrinogen with a frequency of 79% prior to affinity purification and 91% afterward. Fab' from anti-E immunoglobulin attached to the central nodule with a frequency of 78% prior to affinity purification and 82% afterward. The evidence clearly identifies fragment D produced by plasmin or trypsin digestion of fibrinogen with the outer nodules and the single fragment E, with the central nodule.
用人纤维蛋白原经胰蛋白酶消化产生核心片段D和E，并针对分离出的片段制备抗体。将这些抗体衍生的Fab'片段与天然纤维蛋白原混合，形成可溶性免疫复合物。这些复合物用铂进行旋转投影或用醋酸铀酰进行负染色，然后用电子显微镜检查。发现抗D免疫球蛋白的Fab'在亲和纯化前以79%的频率附着于纤维蛋白原的外周结节，亲和纯化后为91%。抗E免疫球蛋白的Fab'在亲和纯化前以78%的频率附着于中央结节，亲和纯化后为82%。该证据清楚地将纤维蛋白原经纤溶酶或胰蛋白酶消化产生的片段D与外周结节以及单个片段E与中央结节联系起来。
