Abstract
Type-I and type-III collagens were obtained by differential salt fractionation of neutral-salt-soluble collagen from rat skin. Their thermal stabilities were determined by u.v. difference spectroscopy. The ‘melting’ temperature (Tm) in 5mm-acetic acid of type-III collagen was almost 2°C above that of type-I collagen. Intramolecular covalent cross-linking had no effect on the thermal stability.
- © 1982 London: The Biochemical Society
April 1982
Volume: 203 Issue: 1
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Difference in thermal stability of type-I and type-III collagen from rat skin
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