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Volumn 40, Issue 22, 2001, Pages 6670-6679

The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activation

(5) Chuang, Y J a Swanson, R a Raja, S M a Bock, S C b Olson, S T a

a UNIVERSITY OF ILLINOIS AT CHICAGO (United States)

b UNIVERSITY OF UTAH SCHOOL OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUTATION;

CHEMICAL ACTIVATION; ENZYME INHIBITION; FLUORESCENCE; POLYSACCHARIDES;

ENZYMES;

ANTITHROMBIN; ARGININE; BLOOD CLOTTING FACTOR 10A; HEPARIN; HISTIDINE; LEUCINE; METHIONINE; MUTANT PROTEIN; PROTEINASE; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; THROMBIN; TRYPTOPHAN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITION; HUMAN; PRIORITY JOURNAL;

ANIMALS; ANTITHROMBINS; ARGININE; BINDING SITES; CELL LINE; CHYMOTRYPSIN; CRICETINAE; ENZYME ACTIVATION; FACTOR XA; HEPARIN; HUMANS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SERINE PROTEINASE INHIBITORS; SERPINS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; THROMBIN;

EID: 0035810925 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi002933d Document Type: Article

Times cited : (53)

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