Abstract
Circular dichroism spectra in the ultraviolet region, similar to the spectrum of the collagen helix, were regenerated when various grades of industrial gelatin were allowed to stand at 5°C in a concentration low enough that they did not form gels. Spectrum generation was decreased by an addition of salt or alcohol and by raising the temperature. Maximal regeneration took place at the respective iso-ionic points "Of the acid- and alkali-processed gelatins. As judged from these spectra, 60% of the helical structure of collagen was regenerated from the industrial gelatin that had the highest α-chain content.
