The amino acid composition of fish collagen and gelatin
- 1 February 1957
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 65 (2) , 363-368
- https://doi.org/10.1042/bj0650363
Abstract
The amino acid compositions of collagens and derived gelatins from sturgeon, cod, the shark (Selachus maximus) and the Australian lung fish were determined. These fish collagens show a similar amino acid distribution to mammalian collagen, with decreased amounts of proline and hydroxyproline, and increased serine, threonine and, in some cases, methionine and hydroxylysine. Gelatin prepared from cod bone has a very low rigidity at 10[degree], whereas sturgeon, shark and lung-fish collagens give rise to gelatins having rigidities of the same order as, but probably somewhat below, those of mammalian gelatins. In general, the shrinkage temperature of the collagen and gel properties of extracted gelatin decrease with decreasing hydroxyproline content. Certain departures in detail from this behavior indicate that other unknown features of composition may influence the stability of linkages between polypeptide chains. Variations in the properties and composition of fish collagens seem related to the water temperature of the normal habitat, rather than to considerations of broad zoological classification.Keywords
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