The pH Dependence of Serpin-Proteinase Complex Dissociation Reveals a Mechanism of Complex Stabilization Involving Inactive and Active Conformational States of the Proteinase Which Are Perturbable by Calcium

Journal of Biological Chemistry

Volumn 276, Issue 35, 2001, Pages 32446-32455

  Calugaru, Sergei V ^b   Swanson, Richard ^b   Olson, Steven T ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CATALYSIS; ESTERS; HYDROLYSIS; PH EFFECTS; POSITIVE IONS; RATE CONSTANTS;

LIGANDS;

ENZYMES;

CALCIUM; GUANIDINE DERIVATIVE; HYDROXIDE; HYDROXYLAMINE; PROTEINASE; SERINE PROTEINASE INHIBITOR; TOSYLARGININE METHYL ESTER; ALPHA 1 ANTITRYPSIN; RECOMBINANT PROTEIN; SERINE PROTEINASE; THROMBIN; TRYPSIN;

ALLOSTERISM; ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DEACYLATION; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; EQUILIBRIUM CONSTANT; HYDROLYSIS; LIGAND BINDING; PH; PRIORITY JOURNAL; AMINO ACID SEQUENCE; CHEMICAL MODEL; CHEMISTRY; HUMAN; KINETICS; METABOLISM; PROTEIN CONFORMATION;

ALPHA 1-ANTITRYPSIN; AMINO ACID SEQUENCE; CALCIUM; ENZYME STABILITY; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; SERPINS; THROMBIN; TRYPSIN;

EID: 0035980118     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M104731200     Document Type: Article

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