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- W1979569213 abstract "α2-Antiplasmin (AP) inhibits plasmin in a two-step reaction in which AP reversibly binds to lysine-binding sites of plasmin and, then, more slowly complexes covalently with the enzyme's active site. Here, we show that the C-terminal lysine residue of AP has a key role in binding of the inhibitor to plasmin. A synthetic peptide corresponding to the C-terminal 26 amino acid residues of AP blocked association of AP with plasmin, but this activity of the peptide was lost when its C-terminal lysine residue was removed with carboxypeptidase B. The essential role of this lysine residue was shown more directly by treating AP with carboxypeptidase B and observing that AP lost its ability to inhibit plasmin rapidly." @default.
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- W1979569213 date "1988-09-01" @default.
- W1979569213 modified "2023-09-28" @default.
- W1979569213 title "α2-antiplasmin's carboxy-terminal lysine residue is a major site of interaction with plasmin" @default.
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- W1979569213 doi "https://doi.org/10.1016/s0006-291x(88)80535-7" @default.
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