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
Language
- eng
Conference Location
- United States