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Abstract
The water-soluble proteins of the human fetal lens (175- and 285-day-old) contain
HM-, pre-alpha-, alpha-, beta- and gamma-crystallins. Using the frozen-sectioning
technique, it can be demonstrated that the fetal lens does not have an homogeneous
distribution of crystallins, but there are gradual differences between the cortices
and the nucleus. The frozen-sectioning technique shows for the adult lens significantly
increasing amounts of beta-crystallins of pI 4.95-5.55, especially at the posterior
supra-nuclear layer, increasing amounts of HM-crystallins and decreasing amounts of
beta-crystallins of pI 5.80-7.05 in the nucleus. This microsectioning technique was
correlated with Scheimpflug photographs of the fetal and adult lens. In the fetal
lens, the anterior capsule and 2 peaks in the anterior and posterior supranuclear
layers could be visualized after densitometry. In the adult lens 5 layers could be
demonstrated, e.g. the anterior capsule, the anterior supranuclear layer, the nucleus,
the posterior supranuclear layer and the anterior capsule.