The effect of divalent cations on the conformation and function of human plasminogen.

Journal Article (Journal Article)

The activation of native human plasminogen (Glu1-Pg) by tissue plasminogen activator, urinary plasminogen activator (u-PA), and streptokinase is inhibited by the divalent cations Ca2+, Mg2+, and Mn2+. This inhibition is accompanied by a conformational change in the molecule as evidenced by a decrease in Stokes' radius and intrinsic fluorescence. Kinetic analysis indicates that Mn2+ acts as an uncompetitive inhibitor of u-PA-catalyzed Glu1-Pg activation. In contrast to the inhibitory effects of divalent cations on Glu1-Pg, Ca2+ and Mg2+ stimulate the activation of proteolytically modified Lys77-Pg. These observations provide further evidence that Glu1-Pg and Lys77-Pg exhibit differential responses to ligands in the microenvironment.

Full Text

Duke Authors

Cited Authors

  • Stack, S; Gonzalez-Gronow, M; Pizzo, SV

Published Date

  • January 1, 1991

Published In

Volume / Issue

  • 284 / 1

Start / End Page

  • 58 - 62

PubMed ID

  • 1899177

International Standard Serial Number (ISSN)

  • 0003-9861

Digital Object Identifier (DOI)

  • 10.1016/0003-9861(91)90263-i


  • eng

Conference Location

  • United States