The entire y-carboxyglutamic acid- and helical stack-domains of human coagulation factor IX are required for optimal binding to its endothelial cell receptor

International Journal of Peptide and Protein Research

Volumn 48, Issue 3, 1996, Pages 281-285

  Prorok, Mary ^a   Geng, Jie Ping ^a   Warder, Scott E ^a   Castellino, Francis J ^a  

^a UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

Cell binding; Cellular receptors; Domain folding; Endothelial cells; Factor IX

Indexed keywords

BLOOD CLOTTING FACTOR 9;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENDOTHELIUM CELL; HUMAN; HUMAN TISSUE; IN VITRO STUDY; NORMAL HUMAN; PEPTIDE SYNTHESIS; PLASMA; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; RECEPTOR BINDING; STRUCTURE ACTIVITY RELATION;

1-CARBOXYGLUTAMIC ACID; ANIMALS; CATTLE; CELLS, CULTURED; ENDOTHELIUM, VASCULAR; FACTOR IX; HUMANS; PROTEIN CONFORMATION; RECEPTORS, CELL SURFACE;

BOVINAE;

EID: 0029774559     PISSN: 03678377     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3011.1996.tb00842.x     Document Type: Article

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