Alpha-2-plasmin inhibitor comprises a single domain

The reaction between plasmin and α 2PI (alpha-2-plasmin inhibitor), which constitutes a major regulatory step in fibrinolysis, involves both interactions between the kringle structures of plasmin and a complementary site on the inhibitor, and also between the inhibitor reactive center and the enzyme...

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Veröffentlicht in:Biochemical and biophysical research communications 1986-09, Vol.139 (3), p.1062-1070
Hauptverfasser: Magnotti, Ralph A., Halsall, H. Brian
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container_title Biochemical and biophysical research communications
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creator Magnotti, Ralph A.
Halsall, H. Brian
description The reaction between plasmin and α 2PI (alpha-2-plasmin inhibitor), which constitutes a major regulatory step in fibrinolysis, involves both interactions between the kringle structures of plasmin and a complementary site on the inhibitor, and also between the inhibitor reactive center and the enzyme active site. An attempt was made to distinguish calorimetrically the two functional domains of α 2PI. Only one transition was seen, both in the DSC and UV experiments, contrary to the expected two. This transition was unaffected by K4 of plasminogen but was abolished in the presence of anhydrotrypsin. This suggests the major domain structure in α 2PI is associated with the reactive center.
doi_str_mv 10.1016/S0006-291X(86)80285-6
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subjects alpha-2-Antiplasmin - metabolism
Applied sciences
Binding Sites
Calorimetry, Differential Scanning
Exact sciences and technology
Fibrinolysin - metabolism
Fibrinolysis
Humans
Other techniques and industries
Ultraviolet Rays
title Alpha-2-plasmin inhibitor comprises a single domain
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