Van Caneghem P, Lapiere C M
C R Seances Soc Biol Fil. 1975;169(1):242-5.
Irradiation of native collagen from lathyric rats in solution reduces the depolymerisation speed in the cold of fibres formed by gelification at 37 degrees C, rendering it thus comparable to the speed observed with normal collagen. In our test this normalisation does not appear if the collagen is irradiated in the state of gel. These observations and the absence of specific modifications induced by irradiation in the presence of reagents of the aldehydes speak in favour of the interference, on irradiation, of chemical groups different from the physiological aldehyde groups.
对患骨生成障碍病大鼠溶液中的天然胶原蛋白进行辐照，可降低其在37℃凝胶化形成的纤维在低温下的解聚速度，从而使其与正常胶原蛋白的解聚速度相当。在我们的试验中，如果胶原蛋白处于凝胶状态下进行辐照，这种正常化现象不会出现。这些观察结果以及在醛类试剂存在下辐照未引起特异性修饰，表明辐照时生理醛基以外的化学基团发生了干扰作用。
