The biosynthesis of basement membrane collagen in embryonic chick lens. 3. Intracellular formation of the triple helix and the formation of aggregates through disulfide bonds.
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abstract
The basement membrane [14C]collagen secreted into the medium by matrix free lens cells was found to be largely resistent to pepsin at 15, suggesting that it was in a triple helical conformation. In contrast, [14C]collagen in the lens cells themselves was largely digested by pepsin at 15, suggesting it was in a random coil form. Gel filtration in sodium dodecyl sulfate showed that the 14C polypeptides of the collagen in the medium were recovered in aggregates greater than 140,000 daltons when reduction with mercaptoethanol was omitted prior to chromatography. With the cell fraction, essentially all of the [14C] collagen polypeptides were found to elute with molecular weights of 140,000, whether or not reduction with mercaptoethanol was carried out. The observations are consistent with the possibility that the formation of disulfide bonds among the polypeptide chains is of considerable importance in promoting the formation of the triple helix.
