Modified crossed immunoelectrophoresis to study with whole plasma the reversible complex formation of histidine-rich glycoprotein with plasminogen.

Abstract:

: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.

journal_name

Thromb Haemost

authors

Kluft C,Los P

subject

Has Abstract

pub_date

1988-12-22 00:00:00

pages

411-4

issue

3

eissn

0340-6245

issn

2567-689X

journal_volume

60

pub_type

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