Alpha 2-antiplasmin's carboxy-terminal lysine residue is a major site of interaction with plasmin.

Abstract:

:alpha 2-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.

authors

Hortin GL,Gibson BL,Fok KF

doi

10.1016/s0006-291x(88)80535-7

subject

Has Abstract

pub_date

1988-09-15 00:00:00

pages

591-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80535-7

journal_volume

155

pub_type

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