Abstract
1. A new type of hyaline, colourless cuticle, called rubber-like cuticle, is described and analysed qualitatively with respect to mechanical behaviour, structure and composition. Externally it is covered by ordinary thin epicuticle, but otherwise it represents the simplest type of cuticle known and consists only of thin continuous lamellae of chitin (0-2 µ) separated and glued together by an elastic protein, resilin, not hitherto described. There are only traces of water-soluble substances present and resilin sometimes occurs as pure, hyaline patches more than 100 µ thick and suitable for macroscopic experiments. 2. In all physical respects, resilin behaves like a swollen isotropic rubber but the rigid experimental proof is given elsewhere (Weis-Fogh, 1961). An outstanding feature is the complete lack of flow not paralleled by other natural or synthetic rubbers. 3. Resilin resembles elastin but it is devoid of colour and has a different and characteristic amino-acid composition (Bailey & Weis-Fogh, 1961). The nature of the cross-linkages is unknown at present but they are extremely stable, of a co-valent type and different from other known cross-linkages in proteins. This accounts for its insolubility and resistance to all agents which do not break the peptide backbone. 4. Resilin is a structure protein in which the primary chains show little or no tendency to form secondary structures; they are bound together in a uniform three-dimensional network (the tertiary structure) with no potential limits as to size.