Spontaneous inactivation of human tryptase involves conformational changes consistent with conversion of the active site to a zymogen-like structure

Biochemistry

Volumn 37, Issue 38, 1998, Pages 13174-13183

  Selwood, Trevor ^a   McCaslin, Darrell R ^a   Schechter, Norman M ^a,b  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBENZAMIDINE; DEXTRAN SULFATE; TRYPTASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME INACTIVATION; FLUORESCENCE; PRIORITY JOURNAL;

BENZAMIDINES; BINDING SITES; BINDING, COMPETITIVE; CHYMASES; DEXTRAN SULFATE; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; ENZYME PRECURSORS; HUMANS; KINETICS; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; SPECTROMETRY, FLUORESCENCE; TRYPTASES;

EID: 0032558456     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980780c     Document Type: Article

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