[HTML][HTML] Isolation and characterization of the kininogen-binding protein p33 from endothelial cells: identity with the gC1q receptor
H Herwald, J Dedio, R Kellner, M Loos… - Journal of Biological …, 1996 - ASBMB
Kininogens, the precursor proteins of the vasoactive kinins, bind specifically, reversibly, and
saturably to platelets, neutrophils, and endothelial cells. Two domains of the kininogens
expose major cell binding sites: domain D3 that is shared by H-and L-kininogen and domain
D5 H that is exclusively present in H-kininogen. Previously we have mapped the kininogen
cell binding sites to 27 residues of D3 (" LDC27") and 20 residues of D5 H (" HKH20"),
respectively (Herwald, H., Hasan, AAK, Godovac-Zimmermann, J., Schmaier, AH, and Müller …
saturably to platelets, neutrophils, and endothelial cells. Two domains of the kininogens
expose major cell binding sites: domain D3 that is shared by H-and L-kininogen and domain
D5 H that is exclusively present in H-kininogen. Previously we have mapped the kininogen
cell binding sites to 27 residues of D3 (" LDC27") and 20 residues of D5 H (" HKH20"),
respectively (Herwald, H., Hasan, AAK, Godovac-Zimmermann, J., Schmaier, AH, and Müller …
