Abstract
Elastoidin, a member of the collagen class of proteins, proves to be a tightly bonded mixture of a characteristic collagen which may be extracted by autoclaving as a water-soluble gelatin, and a water-insoluble, tyrosine-rich residue. The cleaned fibers of three species of selachian fishes yielded 14 to 26% of the insoluble residue, containing 18 to 25% tyrosine.
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