Rat tail tendon (RTT) collagen has been crosslinked with 1% basic chromium
sulfate (BCS) at pH 3.2, and 2, 4, 8, and 10% formaldehyde (HCHO) at pH 5 a
nd pH 8. The viscoelastic behavior (such as stress relaxation behavior for
BCS and HCHO-tanned RTT) has been studied in water and 6M urea at different
temperatures. The total rate of relaxation has been divided into fast and
slow components, and computed using the two-term model and nonlinear least-
squares fit. The rate of relaxation for crosslinked RTT is less than the na
tive one. Activation energy at absolute zero has been computed using k = AT
(m)e(-E0/RT) and nonlinear least-squares fit. The activation energy increas
es for crosslinked RTT than the native one. This is consistent with the obs
erved rate constant values. This may be due to the additional stability imp
arted to RTT collagen by coordinate covalent and covalent crosslinks throug
h BCS and HCHO, respectively. (C) 1999 John Wiley & Sons, Inc.