Synopsis
Sclerotization of skate egg capsule occurs after secretion of capsule precursors from the shell gland and involves a form of quinone tanning in which catechols are introduced in utero and subsequently oxidized to quinones by catechol oxidase. A latent form of enzyme is incorporated in the capsular matrix during secretion. Oxidase activity increases concomitantly with increasing catechol and quinone contents. Six major proteins ranging in size from 95kDa to 20kDa comprise the skate egg capsule, all of which contain elevated levels of glycine, serine, proline and tyrosine. Hydroxyproline occurs in all but one protein, however, none has an amino acid composition typical of collagen. Solubilization of two proteins from pre-tanned capsule requires reducing agents indicating that an early event leading to matrix stabilization is mediated by disulfide bonds. Stabilization of the other proteins along with the disulfide bonded proteins directly correlates with increasing catechol content, catechol oxidase activity and quinone formation.
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Koob, T.J., Cox, D.L. Stabilization and sclerotization ofRaja erinacea egg capsule proteins. Environ Biol Fish 38, 151–157 (1993). https://doi.org/10.1007/BF00842911
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DOI: https://doi.org/10.1007/BF00842911