Russell P, Carper D A, Chiogioji A, Reddy V
Invest Ophthalmol Vis Sci. 1985 Jul;26(7):1028-31.
Three monoclonal antibodies against lens crystallin have been used to study the accumulation of specific polypeptides during development of the human lens. One antibody which recognizes an antigen common to three polypeptides with molecular weights close to 31,000 reacted equally well to the human lens cortex and nucleus and had a similar binding activity to proteins isolated from embryonic and older human lenses. This suggests that the antigen accumulates to the same degree in human lenses during development. The second monoclonal antibody to the 24,000 molecular weight gamma-crystallin showed increased binding at the older ages indicating the increased accumulation of this protein during lens development. The third monoclonal antibody to a beta-crystallin of 27,000 molecular weight showed little if any reactivity at the embryonic age and revealed a clear difference between the binding with cortical and nuclear protein at older ages. It appears that the 27,000 molecular weight beta-crystallin may not be synthesized in the embryonic human lens.
三种针对晶状体结晶蛋白的单克隆抗体已被用于研究人晶状体发育过程中特定多肽的积累情况。一种抗体可识别分子量接近31,000的三种多肽的共同抗原，它与人晶状体皮质和核的反应同样良好，并且与从胚胎期和成年期人晶状体中分离出的蛋白质具有相似的结合活性。这表明该抗原在人晶状体发育过程中积累到相同程度。第二种针对分子量为24,000的γ-晶状体蛋白的单克隆抗体在年龄较大时结合增加，表明该蛋白质在晶状体发育过程中积累增加。第三种针对分子量为27,000的β-晶状体蛋白的单克隆抗体在胚胎期几乎没有反应，并且在年龄较大时显示出与皮质蛋白和核蛋白结合的明显差异。看来分子量为27,000的β-晶状体蛋白可能不在胚胎期人晶状体中合成。
