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Titolo:
SOYBEAN BOWMAN-BIRK PROTEASE INHIBITOR IS A HIGHLY EFFECTIVE INHIBITOR OF HUMAN MAST-CELL CHYMASE
Autore:
WARE JH; WAN XS; RUBIN H; SCHECHTER NM; KENNEDY AR;
Indirizzi:
UNIV PENN,DEPT RADIAT ONCOL,530 CLIN RES BLDG,415 CURIE BLVD PHILADELPHIA PA 19104 UNIV PENN,DEPT MED PHILADELPHIA PA 19104 UNIV PENN,DEPT DERMATOL PHILADELPHIA PA 19104
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 1, volume: 344, anno: 1997,
pagine: 133 - 138
SICI:
0003-9861(1997)344:1<133:SBPIIA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHYMOTRYPSIN-LIKE PROTEINASE; SPONTANEOUS INACTIVATION; CATHEPSIN-G; TRYPTASE; INTERNALIZATION; IDENTIFICATION; CLEAVAGE; SEQUENCE; CANCER; SITE;
Keywords:
HUMAN CHYMASE; HUMAN TRYPTASE; INHIBITION; BOWMAN-BIRK INHIBITOR; SERINE PROTEASE; PROTEASE INHIBITOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
J.H. Ware et al., "SOYBEAN BOWMAN-BIRK PROTEASE INHIBITOR IS A HIGHLY EFFECTIVE INHIBITOR OF HUMAN MAST-CELL CHYMASE", Archives of biochemistry and biophysics, 344(1), 1997, pp. 133-138

Abstract

Soybean Bowman-Birk protease inhibitor (BBI) is an inhibitor of serine proteases with two functional inhibitory domains of different specificities: one is specific for chymotrypsin-like proteases, the other for trypsin-like proteases, Chymase and tryptase are serine proteases which are stored in mast cell granules and released upon degranulation. This work investigated the inhibition of human chymase and tryptase byBBI. Active-site titration of human skin chymase by BBI demonstrated that BBI was a highly effective inhibitor of human chymase, Virtually stoichiometric inhibition of chymase by BBI was observed at 1.0 nM chymase, Kinetic studies of the inhibition reaction yielded an association rate constant of 4.0 x 10(5) M-1 s(-1) and a dissociation rate constant of 1.7 x 10(-5) s(-1). From these two constants we estimate a K-i of 50 pM. Chymase/BBI complexes did not dissociate in SDS-PAGE analyses under nonreducing conditions, consistent with the formation of a very tight complex with little tendency to dissociate. In contrast to chymase, human tryptase was not inhibited by BBI. These studies demonstrate that BBI is a good inhibitor of human chymase, exhibiting reaction properties better than physiological inhibitors described to date. (C)1997 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 10:42:41