MUELLER-EBERHARD H J, BIRO C E
J Exp Med. 1963 Sep 1;118(3):447-66. doi: 10.1084/jem.118.3.447.
Purification of the activity of the fourth component of human complement resulted in the isolation of a highly homogeneous serum protein. Since this protein has not been recorded previously it was called beta(1E)-globulin on the basis of its immunoelectrophoretic behavior. C'4 activity and beta(1E)-globulin were found to have highly similar, if not identical physicochemical characteristics. Moreover, beta(1E)-globulin was shown to exhibit the specific behavior of C'4 activity in that it is taken up only by cells which contain activated C'1. DFP-inactivated C'1 failed to catalyze uptake of the protein. Treatment with hydrazine which is known to destroy C'4 activity, led to changes in the physicochemical properties of beta(1E)-globulin and rendered the molecule incapable to combine with C'1-containing cells. The evidence indicates that beta(1E)-globulin represents the fourth component of human complement.
人补体第四成分活性的纯化导致分离出一种高度均一的血清蛋白。由于此前未记录过这种蛋白,根据其免疫电泳行为将其称为β(1E)-球蛋白。发现C'4活性和β(1E)-球蛋白具有高度相似(即便不是完全相同)的物理化学特性。此外,β(1E)-球蛋白表现出C'4活性的特异性行为,即它仅被含有活化C'1的细胞摄取。二异丙基氟磷酸酯(DFP)灭活的C'1无法催化该蛋白的摄取。用已知会破坏C'4活性的肼处理,导致β(1E)-球蛋白的物理化学性质发生变化,并使该分子无法与含C'1的细胞结合。证据表明β(1E)-球蛋白代表人补体的第四成分。