Szabolcs M, Csabina S, Francia I, Csorba S
Acta Paediatr Hung. 1986;27(3):239-46.
The Ca2+-binding gluten fraction isolated by the authors has been shown to prolong the clearing phase and to shorten the physiological contraction phase of ATP activated natural actomyosin suspension in the presence of physiological potassium chloride in a dose dependent manner. The mean ATPase activity of myosin and actomyosin was calculated for each phase from the actual ATP concentrations, measured at 30 sec intervals, and from the phase lengths. The preparation was found markedly to inhibit the ATPase activity during the clearing and physiological contraction phase. Since both myosin and actomyosin ATPase is Ca2+-dependent, it is assumed that the inhibitory effect of the gluten fraction on ATPase activity may be mediated by its free Ca2+-binding capacity, resulting in modified phase lengths of actomyosin superprecipitation. On the basis of these experimental results a hypothesis is put forward of the part of the Ca2+-binding gluten fraction played in the pathomechanism of coeliac disease.
作者分离出的钙结合麦谷蛋白组分已被证明，在生理氯化钾存在的情况下，能以剂量依赖的方式延长ATP激活的天然肌动球蛋白悬浮液的澄清期，并缩短其生理收缩期。根据每隔30秒测量的实际ATP浓度以及各阶段的时长，计算出每个阶段肌球蛋白和肌动球蛋白的平均ATP酶活性。结果发现，该制剂在澄清期和生理收缩期能显著抑制ATP酶活性。由于肌球蛋白和肌动球蛋白的ATP酶都依赖于钙离子，因此推测麦谷蛋白组分对ATP酶活性的抑制作用可能是由其游离钙离子结合能力介导的，从而导致肌动球蛋白超沉淀的阶段时长发生改变。基于这些实验结果，提出了一个关于钙结合麦谷蛋白组分在乳糜泻发病机制中所起作用的假说。
