Evidence that the fibrinogen binding domain of Apo(a) is outside the lysine binding site of kringle IV-10: a study involving naturally occurring lysine binding defective lipoprotein(a) phenotypes.

It is now established that the lysine binding site (LBS) of apo(a) kringle IV-10, and particularly Trp72, plays a dominant role in the binding of lipoprotein(a) [Lp(a)] to lysine. To determine the role of the LBS in the binding of Lp(a) to fibrinogen, we examined the binding to plasmin-modified (PM)...

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Detalhes bibliográficos
Main Authors: Klezovitch, O, Edelstein, C, Scanu, A M
Formato: Artigo
Idioma:Inglês
Publicado em: 1996
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC507415/
https://ncbi.nlm.nih.gov/pubmed/8690792
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