Modified crossed immunoelectrophoresis to study with whole plasma the reversible complex formation of histidine-rich glycoprotein with plasminogen
article
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 plasminogen at 0.50-0.55 μM 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 α2-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 α2-antiplasminogen in whole plasma. Chemicals/CAS: plasminogen, 9001-91-6; Antiplasmin; Blood Proteins; Glycoproteins; histidine-rich proteins; Plasminogen, 9001-91-6
Topics
TNO Identifier
230749
ISSN
03406245
Source
Thrombosis and Haemostasis, 60(3), pp. 411-414.
Pages
411-414
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