Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation influence of ω-aminocarboxylic acids
S Thorsen - Biochimica et Biophysica Acta (BBA)-Protein Structure, 1975 - Elsevier
Pretreatment of native plasminogen with plasmin or activators resulted in a pronounced
increase in the binding of plasminogen to fibrin. The pretreated plasminogen was
considered to be identical to the proteolytically degraded proenzyme with NH 2-terminal
lysine, valine or methionine, which is formed as an intermediate stage during activation of
plasminogen. Bound plasminogen could be extracted by 6-aminohexanoic acid indicating a
reversible binding between plasminogen and fibrin. Adsorption of pretreated plasminogen …
increase in the binding of plasminogen to fibrin. The pretreated plasminogen was
considered to be identical to the proteolytically degraded proenzyme with NH 2-terminal
lysine, valine or methionine, which is formed as an intermediate stage during activation of
plasminogen. Bound plasminogen could be extracted by 6-aminohexanoic acid indicating a
reversible binding between plasminogen and fibrin. Adsorption of pretreated plasminogen …
