Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: Dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire process

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1385, Issue 1, 1998, Pages 139-148

  Kozik, Andrzej ^a   Potempa, Jan ^a   Travis, James ^b  

^a JAGIELLONIAN UNIVERSITY   (Poland)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

Cross linking; Mast cell; Quaternary structure; Regulatory mechanism; Tryptase

Indexed keywords

TRYPTASE;

ARTICLE; CROSS LINKING; DISSOCIATION; ENZYME DEGRADATION; ENZYME INACTIVATION; GEL PERMEATION CHROMATOGRAPHY; HUMAN; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

BIOPOLYMERS; CHROMATOGRAPHY, GEL; CHYMASES; CROSS-LINKING REAGENTS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME STABILITY; HUMANS; KINETICS; LUNG; MAST CELLS; OSMOLAR CONCENTRATION; SERINE ENDOPEPTIDASES; TEMPERATURE; TRYPTASES;

EID: 0031806935     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00053-3     Document Type: Article

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