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- W2072296215 abstract "Some of the physical properties of collagen from the bovine cornea have been studied and compared with those of collagens from other sources. Polymeric and essentially monomeric collagens were prepared by extraction of the corneas with acetic acid, and the collagens were purified and fractionated on the basis of solubility in solutions of varying salt concentrations. Ultracentrifugal and viscometric studies indicated that the corneal collagen monomer is essentially identical to the monomer of other collagens in respect to size and shape and that the soluble corneal collagen polymers appear to occur as aggregates with axial ratios close to that of the monomer. Native and denatured corneal collagen were found to be similar to native and denatured collagens from other sources in respect to optical rotatory dispersion. Significant differences between corneal and skin collagen were found in their amino acid compositions and in their behavior during thermal denaturation. There appeared to be a definite correlation between the extensive intermolecular cross-linking of the collagen polymer obtained by acid extraction and the increased thermal stability. The differences in amino acid composition could not be related to this observation." @default.
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- W2072296215 date "1967-01-01" @default.
- W2072296215 modified "2023-10-18" @default.
- W2072296215 title "The physical properties of bovine corneal collagen" @default.
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- W2072296215 doi "https://doi.org/10.1016/s0014-4835(67)80054-x" @default.
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