Abstract
The thermal stability of acid-soluble collagens was studied by circular dichroism (CD) spectroscopy. Adult bovine dermal collagen (BDC), rat-tail tendon collagen (RTC), and calf skin collagen (CSC) were compared. Despite some variability in amino acid composition and apparent molecular weight, the CD spectra for helical and unordered collagen structures were essentially the same for all the sources. The melting of these collagens occurs as a two-stage process characterized by a pretransition (Tp) followed by complete denaturation (Td). The characteristic temperatures vary with the source of the collagen; for mature collagens (BDC, RTC) Tp = 30 degrees C and Td = 36 degrees C, and for CSC Tp = 34 degrees C and Td = 40 degrees C. Neutral salts, NaCl or KCl, at low concentrations (0.02-0.2 M) appear to bind to the collagens and shift the thermal transitions of these collagens to lower temperatures.
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