Abstract

During growth of the eye lens, epithelial cells differentiate into fibre cells under the influence of neural retina. The fibre differentiation factor (FDF) was partially characterized from calf retina-conditioned medium, using lens epithelial explants from young rats, to provide a bioassay for differentiation. FDF was associated with large-protein aggregates, the smallest of which eluted at ~500–600 kD on Sephacryl S-300 columns and migrated as a single protein band near 600 kD on gradient gels. This protein resolved into nine major peptides on SDS-polyacrylamide gels, ranging between 23 and 27 kD. Eight of these peptides were present as four doublets, but did not appear to contain specific carbohydrate residues. The ~500–600 kD complex could be slightly disrupted by trypsin or heat treatment to release a less stable 90 kD component. Fractionation of FDF invariably led to loss of activity, possibly due to gradual dissociation into less active and/or less stable components. A working hypothesis suggested by these findings is that FDF is associated with a small group of peptides, each contributing an essential function to the process of fibre differentiation.

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