EXPRESSION AND PURIFICATION OF HUMAN INTERLEUKIN-1-BETA CONVERTING-ENZYME FROM TRICHOPLUSIA NI INSECT CELLS USING A BACULOVIRUS EXPRESSION SYSTEM

Authors
CHEN WY RAYBUCK SA FULGHUM JR PETRILLO RA MARGOLIN N CHAMBERS SP
Citation
Wy. Chen et al., EXPRESSION AND PURIFICATION OF HUMAN INTERLEUKIN-1-BETA CONVERTING-ENZYME FROM TRICHOPLUSIA NI INSECT CELLS USING A BACULOVIRUS EXPRESSION SYSTEM, Protein expression and purification, 9(1), 1997, pp. 69-75
Citations number
30
Categorie Soggetti
Biology,"Biochemical Research Methods
Journal title
Protein expression and purification → ACNP
ISSN journal
10465928
Volume
9
Issue
1
Year of publication
1997
Pages
69 - 75
Database
ISI
SICI code
1046-5928(1997)9:1<69:EAPOHI>2.0.ZU;2-6
Abstract
Employing a baculovirus expression system, human interleukin-1 beta co nverting enzyme (ICE) has been expressed in Trichoplusia ni High-Five insect cells and purified. ICE was expressed with an N-terminal T7 epi tope, thus allowing its purification using immobilized anti-T7 antibod ies. The recombinant ICE was purified to >95% homogeneity, the one min or contaminant being the baculovirus anti-apoptotic protein (P35) whic h was copurified. The purified recombinant ICE was biologically active , cleaving both pIL-1 beta and poly(ADP-ribose) polymerase substrates. The kinetic properties of the purified recombinant ICE compare favora bly with native ICE purified from a THP-1 monocytic line. (C) 1997 Aca demic Press.