Identification of the domains of tissue-type plasminogen activator involved in the augmented binding to fibrin after limited digestion with plasmin
C de Vries, H Veerman, H Pannekoek - Journal of Biological Chemistry, 1989 - ASBMB
The binding of recombinant tissue-type plasminogen activator (rt-PA) to fibrin increases
upon digestion of fibrin with plasmin. Optimal binding is observed following a limited plasmin
digestion of fibrin, coinciding with the generation of fibrin fragment X polymers. We studied
the involvement of the separate domains of the amino-terminal" heavy"(H) chain of rt-PA in
this augmentation of fibrin binding. The fibrin-binding characteristics of a set of rt-PA deletion
mutants, lacking either one or more of the structural domains of the H chain, were …
upon digestion of fibrin with plasmin. Optimal binding is observed following a limited plasmin
digestion of fibrin, coinciding with the generation of fibrin fragment X polymers. We studied
the involvement of the separate domains of the amino-terminal" heavy"(H) chain of rt-PA in
this augmentation of fibrin binding. The fibrin-binding characteristics of a set of rt-PA deletion
mutants, lacking either one or more of the structural domains of the H chain, were …
