Temporary Changes in the dc ElectricalConductivity of MX (3-Chloro-4(Dichloromethyl)-5-Hydroxy-2(5H)-Furanone) Treated Collagen
Temporary Changes in the dc ElectricalConductivity of MX (3-Chloro-4(Dichloromethyl)-5-Hydroxy-2(5H)-Furanone) Treated Collagen
复制标题
MX（3-Chloro-4（二氯甲基）-5-羟基-2（5H）-呋喃酮）处理的胶原蛋白直流电导率的暂时变化
DOI：
10.1023/a:1014298301405
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发表时间：
2001
影响因子：
1.8
通讯作者：
P. Andrzejewski
中科院分区：
文献类型：
--
作者：
L. Kubisz;P. Andrzejewski
本文研究了MX（3-Chloro-4（Dichloromethyl）-5-Hydroxy-2（5 H）- Furanone）对胶原蛋白直流电导率随时间变化的影响。用高效液相色谱法测定MX浓度，胶原蛋白溶液中MX浓度降至初始值的10%，而对照溶液中MX浓度降至初始值的70%。测量了295- 453 K温度范围内的电导率，计算了电荷传导过程的活化能。在295 - 340 K温度范围内，MX的存在降低了胶原的电导率。在295- 320 K温度范围内，活化能随时间降低，这可能是由于胶原-水-MX体系中存在较强的相互作用。在320-410和430 - 450 K温度范围内，活化能与时间无关，MX的应用不改变胶原大分子的结构。在较低温度下发生的暂时变化仅仅是由于胶原-水相互作用的变化。
The influence of MX(3-Chloro-4(Dichloromethyl)-5-Hydroxy-2(5H)- Furanone), a stronglymutagenic compound, on the temperature dependence of the dcelectrical conductivity of collagen as a function of time was studied.Collagen was immersed in MX solution, next dried and pressed intotablets. The MX concentration was measured by HPLC analysis.The reduction of MX concentration to 10% of the initial value wasobserved in the presence of collagen in the solution, whereas in thecontrol solution concentration of MX decreased to 70% of the initialvalue. Measurements of electrical conductivity were performed for thetemperature range 295–453K and activation energies for the chargeconduction process were calculated. Within the temperature range295–340K, the presence of MX decreased electrical conductivity ofcollagen. Calculated activation energies were typical for dry proteins.Within the temperature range 295–320K activation energy decreasedwith time, probably due to the stronger interactions in thecollagen-water-MX system. For temperatures between 320–410 and430–450K the activation energy was not time dependent and theapplication of MX did not change the structure of the collagenmacromolecule. The temporary changes occurring at the lowertemperatures being due solely to changes in the collagen-waterinteractions.