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.

Lignende værker

• Proposed mechanisms for binding of apo[a] kringle type 9 to apo B-100 in human lipoprotein[a].
  af: Guevara, J, et al.
  Udgivet: (1993)
• Rhesus monkey lipoprotein(a) binds to lysine Sepharose and U937 monocytoid cells less efficiently than human lipoprotein(a). Evidence for the dominant role of kringle 4(37).
  af: Scanu, A M, et al.
  Udgivet: (1993)
• High resolution structure of human apolipoprotein (a) kringle IV type 2: beyond the lysine binding site
  af: Santonastaso, Alice, et al.
  Udgivet: (2020)
• Plasma Ip(a) concentration is inversely correlated with the ratio of Kringle IV/Kringle V encoding domains in the apo(a) gene.
  af: Gavish, D, et al.
  Udgivet: (1989)
• Lysine-50 is a likely site for anchoring the plasminogen N-terminal peptide to lysine-binding kringles.
  af: An, S. S., et al.
  Udgivet: (1998)