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      Comparative Studies on Collagens from Bovine and Calf Cornea and Skin

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          Abstract

          The presence of a cross-linking interaction beyond the terminal region of the molecule was established in corneal collagen. The sequence of the terminal regions of corneal collagen did not differ substantially from the sequence in the skin collagen preparations, though minor differences could not be excluded. Most of the skin preparations of insoluble collagen contain tightly attached peptidic material, which was found to be absent in the corresponding corneal preparations. Whether the high resistance of corneal collagen to the solubilizing agents is due to the presence of glycosaminoglycans remains unclear. It has been proved that they are very tightly bound to the insoluble fraction.

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          Author and article information

          Journal
          ORE
          Ophthalmic Res
          10.1159/issn.0030-3747
          Ophthalmic Research
          S. Karger AG
          0030-3747
          1423-0259
          1972
          1972
          09 December 2009
          : 3
          : 5
          : 298-306
          Affiliations
          Eye Research Laboratory and Physiological Institute of the Czechoslovak Academy of Sciences, Prague; Research Institute of Food Industry, Prague
          Article
          266219 Ophthal Res 1972;3:298–306
          10.1159/000266219
          © 1972 S. Karger AG, Basel

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          Pages: 9
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