Lipoprotein a inhibits streptokinase-mediated activation of human plasminogen

Lipoprotein a [Lp(a)] inhibits human plasminogen (Pg) conversion to plasmin (Pm) by streptokinase- (SK-) mediated activation. Kinetic and binding studies indicate that Lp(a) inhibits Pg activation by competitive and uncompetitive inhibition. Lp(a) competes with Pg for SK and forms a stable complex....

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Bibliographic Details
Published in:Biochemistry (Easton) 1989-03, Vol.28 (6), p.2370-2374
Main Authors: Edelberg, Jay M, Gonzalez-Gronow, Mario, Pizzo, Salvatore V
Format: Article
Language:English
Subjects:
Chromatography, Gel
Humans
Kinetics
Lipoprotein(a)
Lipoproteins - isolation & purification
Lipoproteins - metabolism
Plasminogen - metabolism
Plasminogen Activators
Protein Binding
Streptokinase - antagonists & inhibitors
Streptokinase - isolation & purification
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Summary:Lipoprotein a [Lp(a)] inhibits human plasminogen (Pg) conversion to plasmin (Pm) by streptokinase- (SK-) mediated activation. Kinetic and binding studies indicate that Lp(a) inhibits Pg activation by competitive and uncompetitive inhibition. Lp(a) competes with Pg for SK and forms a stable complex. Lp(a) does not, however, inhibit Pg activation by the proteolytic SK-Pm complex. The SK-Pg and SK-Pg(act) intermediate complexes are possible targets of the Lp(a) uncompetitive inhibition. The competitive inhibition constant (Kic) is 45 nM or 14 mg/dL, and the uncompetitive inhibition constant (Kiu) is 140 nM or 42 mg/dL, corresponding to physiologic and pathophysiologic Lp(a) concentrations, respectively.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00432a004