Protonation state of a single histidine residue contributes significantly to the kinetics of the reaction of plasminogen activator inhibitor-1 with tissue-type plasminogen activator

Journal of Biological Chemistry

Volumn 279, Issue 22, 2004, Pages 23007-23013

  Komissarov, Andrey A ^a,c   Declerck, Paul J ^b   Shore, Joseph D ^a  

^a HENRY FORD HEALTH SYSTEM   (United States)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c Henry Ford Health Science Center   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME KINETICS; ENZYMES; ONCOLOGY; PH EFFECTS; RATE CONSTANTS; REACTION KINETICS; TISSUE;

FLUOROMETRY; PROTONATION; SPECIFICITY CONSTANTS;

BIOCHEMISTRY;

HISTIDINE; MONOCLONAL ANTIBODY; N [[2 (IODOACETOXY)ETHYL] N METHY]AMINO 7 NITROBENZ 2 OXA 3 DIAZOLE; PANCREATIC ELASTASE; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEINASE; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; UROKINASE;

ANTIBODY SPECIFICITY; ARTICLE; CARCINOGENESIS; CATALYSIS; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; FLUOROMETRY; NONHUMAN; PH; PRIORITY JOURNAL; PROTON TRANSPORT;

BINDING SITES; CATALYSIS; HISTIDINE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEIN BINDING; TISSUE PLASMINOGEN ACTIVATOR;

INSERTION SEQUENCES;

EID: 2542490214     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401383200     Document Type: Article

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