Rovel A, Rovel B, Vigneron C, Streiff F
Ann Biol Clin (Paris). 1979;37(3):151-6.
The simultaneous study of dynamic and cinematic viscosity in 34 control sera and 49 paraprotein sera showed that there was a simple relationship between the viscosity and the total serum protein content both in normal sera and in paraprotein sera. When the ratio of monoclonal immunoglobulins/total proteins is less than 55%, the viscosity is little or not modified in the case of the IgGk paraproteins studied, whereas it was increased in the case of IgA, IgM and IgG LAMBDA SERA. Beyond 2 cSt, it is not however possible to incriminate a particular type of heavy chain nor even a light chain. The measurement of the viscosity in relation to the temperature permitted us to show that the IgA, IgG, and IgM sera studied all presented an activation energy of outflow (E in Kcal) higher than that of normal sera and the highest rise is due to IgA paraproteins. The concept of energy activation permits us to say that paraproteins have a different behaviour from normal proteins, probably due to disorders in their structural arrangement.
对34份对照血清和49份副蛋白血清进行动态黏度和运动黏度的同步研究表明,正常血清和副蛋白血清的黏度与血清总蛋白含量之间存在简单关系。当单克隆免疫球蛋白/总蛋白的比例小于55%时,在所研究的IgGκ副蛋白情况下,黏度几乎没有改变或未被改变,而在IgA、IgM和IgGλ血清中黏度则升高。然而,超过2厘沲时,则无法确定是某一特定类型的重链,甚至也无法确定是轻链。对与温度相关的黏度测量使我们能够表明,所研究的IgA、IgG和IgM血清的流出活化能(E,千卡)均高于正常血清,且升高幅度最大的是IgA副蛋白。能量活化的概念使我们能够说,副蛋白具有与正常蛋白不同的行为,这可能是由于其结构排列紊乱所致。