Polack B, Valiron O, Concord E, Freyssinet J M, Hudry-Clergeon G
Clin Chem. 1984 Dec;30(12 Pt 1):2093-7.
We examined normal and abnormal fibrinogen (fibrinogen "Grenoble") by two-dimensional gel electrophoresis to obtain data on possible defects at the molecular level. Fibrinogen Grenoble is characterized by an abnormal rate of fibrin monomer aggregation. The electrophoretic analysis revealed the presence of abnormal gamma chains. Two kinds of gamma chains can be detected in fibrinogen Grenoble: (a) normal gamma chains and (b) gamma chains Grenoble (gamma G) with a greater molecular mass but no modification in isoelectric point. The latter chain can be detected in whole plasma by two-dimensional gel electrophoresis. Metrological analysis was performed in an attempt to quantify observed differences between normal fibrinogen and fibrinogen Grenoble. On use of gels stained either with Coomassie Brilliant Blue or with silver, the partly qualified evaluation gives about 60% normal gamma chain and 40% gamma chain Grenoble.
我们通过二维凝胶电泳检查了正常和异常纤维蛋白原（“格勒诺布尔纤维蛋白原”），以获取分子水平上可能存在的缺陷的数据。格勒诺布尔纤维蛋白原的特征是纤维蛋白单体聚集速率异常。电泳分析显示存在异常的γ链。在格勒诺布尔纤维蛋白原中可检测到两种γ链：（a）正常γ链和（b）分子量更大但等电点无改变的格勒诺布尔γ链（γG）。通过二维凝胶电泳可在全血中检测到后一种链。进行了计量分析，试图量化正常纤维蛋白原与格勒诺布尔纤维蛋白原之间观察到的差异。使用考马斯亮蓝或银染色的凝胶时，部分定量评估得出约60%的正常γ链和40%的格勒诺布尔γ链。
