ABSTRACT
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.
