Kluft C, Los P
Gaubius Institute TNO, Leiden, The Netherlands.
Thromb Haemost. 1988 Dec 22;60(3):411-4.
To study the reversible complex formation between the plasma protein histidine-rich glycoprotein (HRG) and plasminogen, crossed immunoelectrophoresis of HRG was modified. In the modification, purified plasminogen was introduced into the gel of the first dimension electrophoresis. Two molecular forms of plasminogen, Glu- and Lys-plasminogen, induced a dose-dependent reduction of the electrophoretic mobility of HRG, with a half maximal retardation for both plasminogens at 0.50-0.55 microM of added plasminogen to the agarose gel. HRG in plasma behaved as a uniform fraction with respect to plasminogen binding. In contrast, with the same modified technique another plasma protein, alpha 2-antiplasmin, separated into a retarded plasminogen-binding form and a non-retarded non-plasminogen-binding form. The method can be used to assess several aspects of reversible complex formation between plasma proteins, as demonstrated for plasminogen binding of HRG and alpha 2-antiplasmin in whole plasma.
为研究血浆蛋白富组氨酸糖蛋白（HRG）与纤溶酶原之间可逆复合物的形成，对HRG的交叉免疫电泳进行了改进。在改进过程中，将纯化的纤溶酶原引入一维电泳凝胶中。两种分子形式的纤溶酶原，即谷氨酸纤溶酶原和赖氨酸纤溶酶原，均可导致HRG电泳迁移率呈剂量依赖性降低，在向琼脂糖凝胶中添加0.50 - 0.55微摩尔纤溶酶原时，两种纤溶酶原均使HRG的迁移率降低一半。血浆中的HRG在纤溶酶原结合方面表现为单一成分。相比之下，采用相同的改进技术，另一种血浆蛋白α2 - 抗纤溶酶则分离为一种迁移受阻的纤溶酶原结合形式和一种迁移不受阻的非纤溶酶原结合形式。该方法可用于评估血浆蛋白之间可逆复合物形成的多个方面，如在全血中HRG和α2 - 抗纤溶酶与纤溶酶原的结合情况所示。
