Abstract
Collagens (acid-solubilized and pepsin-solubilized collagens) were prepared from ocellate puffer fish skin and partially characterized.
With respect to the pepsin-solubilized collagen, it was a heterotrimer with a chain composition of (a1)2a2. The patterns of
peptide fragments were different from skin collagens of other species. The denaturation temperature was 28 C, about 9 C lower
than that of porcine skin collagen. On the other hand, the yields of acid-solubilized and pepsin-solubilized collagens were very
high, 10.7% and 44.7%, respectively, on a dry weight basis. These results suggest that ocellate puffer fish skin has potential as an
alternative source of collagen for use in various fields.