Journal article
A High Affinity Interaction of Plasminogen with Fibrin Is Not Essential for Efficient Activation by Tissue-type Plasminogen Activator*
Abstract
Fibrin (Fn) enhances plasminogen (Pg) activation by tissue-type plasminogen activator (tPA) by serving as a template onto which Pg and tPA assemble. To explore the contribution of the Pg/Fn interaction to Fn cofactor activity, Pg variants were generated and their affinities for Fn were determined using surface plasmon resonance (SPR). Glu-Pg, Lys-Pg (des(1-77)), and Mini-Pg (lacking kringles 1-4) bound Fn with K(d) values of 3.1, 0.21, and 24.5 …
Authors
Kim PY; Tieu LD; Stafford AR; Fredenburgh JC; Weitz JI
Journal
Journal of Biological Chemistry, Vol. 287, No. 7, pp. 4652–4661
Publisher
Elsevier
Publication Date
2 2012
DOI
10.1074/jbc.m111.317719
ISSN
0021-9258