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Titolo:
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
Autore:
KOZIK A; POTEMPA J; TRAVIS J;
Indirizzi:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30602 UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL ATHENS GA 30602 JAGIELLONIAN UNIV,INST MOL BIOL PL-31120 KRAKOW POLAND
Titolo Testata:
Biochimica et biophysica acta. Protein structure and molecular enzymology
fascicolo: 1, volume: 1385, anno: 1998,
pagine: 139 - 148
SICI:
0167-4838(1998)1385:1<139:SIOHLT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAST-CELL TRYPTASE; HUMAN-SKIN TRYPTASE; PROTEASE; CHYMASE; PURIFICATION; ACTIVATION; DEPENDENCE; SEPARATION; HEPARIN;
Keywords:
TRYPTASE; MAST CELL; REGULATORY MECHANISM; QUATERNARY STRUCTURE; CROSS-LINKING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
A. Kozik et al., "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, 1385(1), 1998, pp. 139-148

Abstract

A unique property of human mast cell tryptase is its spontaneous inactivation, which may be relevant to the regulation of the activity of this enzyme in vivo. We have found, using size-exclusion chromatography, that the dissociation of the tetrameric active enzyme into the inactive monomer occurred immediately from the beginning of the inactivation process and at a rate significantly faster than that of the appearance of the inactive, tetrameric form. Eventually, a relatively long-lived state of apparent equilibrium between all three forms (active tetramer, inactive monomer, inactive tetramer) was reached. When tryptase was extensively cross-linked with several heterobifunctional photoactivatable reagents, this modified enzyme exhibited a long-term stability in low-ionic-strength buffer and at elevated temperature, unlike that of the native enzyme. Its is suggested that cross-linking prevents thespontaneous inactivation and dissociation of tryptase by 'freezing' the normal association state of the enzyme and supports the hypothesis that the dissociation of native tetrameric tryptase into inactive monomer is the primary event for the entire process of spontaneous inactivation of this enzyme. (C) 1998 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/10/20 alle ore 04:47:14