Cardone B, Roots B I
Department of Zoology, University of Toronto, Canada.
Neurochem Res. 1996 Apr;21(4):505-10. doi: 10.1007/BF02527716.
Monoclonal antibodies were generated to the proteins in myelin-like membranes isolated from the nerve cords of the earthworm, Lumbricus terrestris. One of these showing cross-reactivity to 30-32 and 40 kDa proteins was shown by immunofluorescence microscopy and immunogold electron microscopy to be bound primarily to glial cell process and their membranes and the myelin-like layers. This antibody cross-reacted with proteins of 60-65, 42, and 40 kDa in crayfish (Procambarus clarki) nerve cord homogenates. Localization by immunoelectron microscopy showed the antibody to be bound exclusively to the membranes of the glial processes ensheathing the axons in the crayfish nerve cord. Thus, the proteins in earthworm and crayfish glial cell membranes have some epitopes in common. We suggest that this may represent an evolutionary conservation of these proteins.
针对从蚯蚓(地龙)神经索中分离出的类髓鞘膜中的蛋白质制备了单克隆抗体。其中一种对30 - 32 kDa和40 kDa蛋白质具有交叉反应性的抗体,通过免疫荧光显微镜和免疫金电子显微镜显示,主要与神经胶质细胞突起及其膜以及类髓鞘层结合。该抗体与小龙虾(克氏原螯虾)神经索匀浆中的60 - 65 kDa、42 kDa和40 kDa蛋白质发生交叉反应。免疫电子显微镜定位显示该抗体仅与包裹小龙虾神经索轴突的神经胶质突起的膜结合。因此,蚯蚓和小龙虾神经胶质细胞膜中的蛋白质具有一些共同的表位。我们认为这可能代表了这些蛋白质的进化保守性。