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Interaction of human plasmin with human alpha sub(2)-macroglobulin
The steady-state kinetic parameters of plasmin and the alpha sub(2)-macroglobulin ( alpha sub(2)M)-plasmin complex toward the chromogenic substrate Val-Leu-Lys-p-nitroanilide (S-2251), in the presence and absence of plasmin competitive inhibitors, have been determined. Two different monoclonal antib...
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Published in: | Biochemistry (Easton) 1984-01, Vol.23 (1), p.105-111 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | The steady-state kinetic parameters of plasmin and the alpha sub(2)-macroglobulin ( alpha sub(2)M)-plasmin complex toward the chromogenic substrate Val-Leu-Lys-p-nitroanilide (S-2251), in the presence and absence of plasmin competitive inhibitors, have been determined. Two different monoclonal antibodies, 10-H-2 and 10-V-1, to the kringle 1-3 region of human plasmin(ogen) and one monoclonal antibody, 10-F-1, to the kringle 4 region of this same enzyme were employed to analyze the topography of plasmin when complexed by alpha sub(2)M. It is concluded that, while slight differences exist in the accessibility or conformation of the plasmin epitopes for these antibodies in the alpha sub(2)M-plasmin complex, a significant portion of plasmin heavy chain is in contact with solvent in the alpha sub(2)M-plasmin complex. |
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ISSN: | 0006-2960 |