Abstract
Bovine corneal and scleral tissues were fractionated to yield acid soluble, alkali soluble, and insoluble collagen preparations. Very small differences in analytical composition were found. The most significant observations were the increased amounts of both acid soluble collagen and non-collagenous soluble proteins found in the cornea, the presence of the latter indicating a larger amount of corneal ground substance. Collagen preparations from both tissues showed comparable susceptibility to digestion by collagenase, and resistance to the action of trypsin.
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