Proteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg1545 optimizes cofactor function by facilitating factor Xa binding

Biochemistry

Volumn 37, Issue 34, 1998, Pages 11896-11906

  Camire, Rodney M ^a,b   Kalafatis, Michael ^a,c   Tracy, Paula B ^a  

^a UNIVERSITY OF VERMONT   (United States)

^b CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^c CLEVELAND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5; CATHEPSIN G; ELASTASE;

ARTICLE; BLOOD CLOTTING; ENZYME BINDING; MOLECULAR DYNAMICS; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ARGININE; BINDING SITES; BLOOD COAGULATION TESTS; CATALYSIS; CATHEPSINS; ENZYME ACTIVATION; FACTOR V; FACTOR VA; FACTOR XA; HUMANS; HYDROLYSIS; KINETICS; MEMBRANES, ARTIFICIAL; PANCREATIC ELASTASE; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLSERINES; PROTEIN BINDING; PROTEIN C; PROTHROMBIN; SERINE ENDOPEPTIDASES;

FELIS CATUS;

EID: 0032566343     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980520v     Document Type: Article

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