Some Properties of Insoluble Bovine Corneal Collagen

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Abstract
Some properties of insoluble corneal collagen were studied using the specific depolymerization action of pronase, pepsin, bacterial α-amylase, 6 M urea, 2% semicarbazide, 2% semicarbazide in combination with 0,5 M Na2CO3, and 0,5 M Na2CO3 alone. Pronase and pepsin released 1.9 % and 1.2 % of the telopeptides in bovine corneal collagen similar to the amount released from other connective tissues (skin 2.6% and 1.9%). Pronase, pepsin and α-amylase solubilized 8.8 %, 2.1%, 24.7 % of insoluble bovine corneal collagen, respectively. It can be concluded that cross-links in corneal collagen are located in the body of the collagen molecule and not in the telopeptide region. The results of the polyacrylamide gel electrophoresis indicate that the α2 chain is presumably much more involved in the cross-linking interactions than α1 The only way to solubilize bovine corneal collagen is the simultaneous treatment of the collagen with semicarbazide and Na2CO3, at pH 10, which seems to be a useful tool for further structural studies of collagen in this tissue.