The effect of ε{lunate}-amino caproic acid on the gross conformation of plasminogen and plasmin

  • Violand B
  • Sodetz J
  • Castellino F
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Previous studies from several laboratories have demonstrated that the native form of circulating plasminogen, Pga, undergoes a gross conformational alteration upon binding the amino acid, ε{lunate}-amino caproic acid (ε{lunate}-ACA), and its analogues. Sedimentation velocity measurements show that plasminogen b Pgb), prepared by removal of a peptide of Mr6000-8000 from the amino terminus of Pga as a consequence of its activation to plasmin, possesses a strikingly dissimilar gross conformation when compared to Pga. However, the overall conformation of Pgb is very similar to the Pga· ε{lunate}-ACA complex. Although Pgb retains its full capacity for binding ε{lunate}-ACA, no additional gross conformational alteration results as a consequence of saturating the binding site of Pgb with this amino acid. Similar measurements show that plasmin a (Pga), which is a direct activation product of Pga, displays a native gross conformation which is very similar to native Pga. Pma binds ε{lunate}-ACA in an identical manner to Pga and also undergoes a similar conformational alteration as Pga, as a consequence of this binding. On the other hand, plasmin b (Pga), which is a direct activation product of Pgb, and also results from removal of the above mentioned peptide from Pma, possesses an overall gross conformation similar to Pgb, the Pga·ε{lunate}-ACA complex and the Pma·ε{lunate}-ACA complex. Although Pmb also retains full capabilities for binding ε{lunate}-ACA, there is no further gross conformational alteration as a result of this interaction. These studies illustrate the importance of the amino terminal region of the original Pga in controlling the overall conformation of the molecule as well as controlling the conformation achieved upon saturation of the molecule by ε{lunate}-ACA like molecules. © 1975.

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