Table 1.
Fibril-forming properties of different types of collagen.
Acid-soluble | Enzyme-treated | Alkali-treated | |
---|---|---|---|
Molecular structure | intact | telopeptides cleaved | deamidized asparagine and glutamine amino acids and telopeptides cleaved |
Gelation | Possible at low concentration of collagen | Possible at high concentration of collagen | at acidic pH with the appearance of non-banded filaments |
Ability to form native banded fibrils | Yes | Yes, but less well organized | No |
Adhesion of cells to substrata from this type of collagen | Good | Good | Good |
Advantages | Ability to form native banded well-ordered collagen fibrils at optimal conditions Ability to form stable collagen gels at very low concentration of collagen |
Ability to form collagen gels with a high concentration of collagen Obliquely banded fibrils, FLS and SLS can be obtained |
Suitable for the production of non-fibrous collagen materials (films, sponge, etc.) |