Monboisse J C, Gardès-Albert M, Randoux A, Borel J P, Ferradini C
Laboratory of Biochemistry, CNRS UA 610, UFR Medicine, Reims, France.
Biochim Biophys Acta. 1988 Apr 14;965(1):29-35. doi: 10.1016/0304-4165(88)90147-x.
Delipidated collagen fibrils reconstituted from acid-soluble calf skin collagen, suspended in 50 mM phosphate buffer, pH 7.4, containing 100 mM sodium formate, were submitted to pulse radiolysis in Febetron devices or to gamma radiolysis in a 60Co irradiator. A collagen degradation process was found. The kinetics of this degradation was followed by evaluation of the amount of 4-hydroxyproline present in the small peptides liberated during the irradiation period. The yield of 4-hydroxyproline small peptides was low (0.1 mol/100 eV for an initial collagen concentration 3.2 microM). It increased linearly with the dose of irradiation and the concentration of collagen in suspension. The kinetic competition between O2-. dismutation and O2-. reaction with collagen was studied by pulse radiolysis at several concentrations of collagen. A value of the kinetic constant of k(O2-. + collagen) = 4.8 . 10(6) mol-1.l.s-1 was determined.
将由酸溶性小牛皮胶原蛋白重组成的脱脂胶原纤维悬浮于含100 mM甲酸钠的50 mM磷酸盐缓冲液（pH 7.4）中，在Febetron装置中进行脉冲辐解，或在60Co辐照器中进行γ辐解。发现了胶原降解过程。通过评估辐照期间释放的小肽中4-羟脯氨酸的含量来跟踪这种降解的动力学。4-羟脯氨酸小肽的产率较低（初始胶原浓度为3.2 μM时为0.1 mol/100 eV）。它随辐照剂量和悬浮液中胶原浓度呈线性增加。通过在几种胶原浓度下进行脉冲辐解研究了O2-歧化与O2-与胶原反应之间的动力学竞争。确定了k(O2- + 胶原) = 4.8×10(6) mol-1·l·s-1的动力学常数。
