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Viscoelastic behavior of formaldehyde and basic chromium sulfate-crosslinked collagen

机译:甲醛和碱性硫酸铬交联胶原蛋白的粘弹性行为

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摘要

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 and pH 8. The viscoelastic behavior (such as stress relaxation behavior for BCS and HCHO-tanned RTT) has been studied in water and 6 M 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 native one. Activation energy at absolute zero has been computed using k = ATme-E(0)/RT and nonlinear least-squares fit. The activation energy increases for crosslinked RTT than the native one. This is consistent with the observed rate constant values. This may be due to the additional stability imparted to RTT collagen by coordinate covalent and covalent crosslinks through BCS and HCHO, respectively.
机译:大鼠尾腱(RTT)胶原蛋白已在pH 3.2时与1%的碱性硫酸铬(BCS)以及在pH 5和pH 8时与2、4、8、10%的甲醛(HCHO)交联。粘弹性行为(例如在水和6 M尿素中,在不同温度下研究了BCS和HCHO鞣制的RTT的应力松弛行为。总松弛率已分为快速和慢速两个部分,并使用二项模型和非线性最小二乘拟合计算。交联的RTT的松弛率小于天然的RTT。已使用k = ATme-E(0)/ RT和非线性最小二乘拟合计算了绝对零时的活化能。交联RTT的活化能比天然RTT高。这与观察到的速率常数值一致。这可能是由于分别通过BCS和HCHO配位共价和共价交联而赋予RTT胶原的额外稳定性。

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