Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate

Journal of Biological Chemistry

Volumn 277, Issue 48, 2002, Pages 46191-46196

  Orcutt, Steven J ^a   Pietropaolo, Concetta ^c   Krishnaswamy, Sriram ^a,b  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BLOOD; CATALYSIS; CHEMICAL BONDS; MUTAGENESIS; SUBSTRATES;

BLOOD COAGULATION;

ENZYMES;

BLOOD CLOTTING FACTOR 10A; SERINE PROTEINASE;

ARTICLE; BINDING AFFINITY; BLOOD CLOTTING; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN INTERACTION;

CULTURE MEDIA, CONDITIONED; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; KINETICS; MUTAGENESIS; PROTHROMBIN; SUBSTRATE SPECIFICITY; THROMBOPLASTIN;

EID: 2242455930     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M208677200     Document Type: Article

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