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Titolo:
PURIFICATION AND CHARACTERIZATION OF RECOMBINANT HUMAN CYCLOOXYGENASE-2
Autore:
PERCIVAL MD; OUELLET M; VINCENT CJ; YERGEY JA; KENNEDY BP; ONEILL GP;
Indirizzi:
MERCK FROSST CTR THERAPEUT RES,DEPT BIOCHEM,POB 1005 POINTE CLAIRE H9R 4P8 PQ CANADA MERCK FROSST CTR THERAPEUT RES,DEPT BIOL MOLEC POINTE CLAIRE H9R 4P8 PQ CANADA MERCK FROSST CTR THERAPEUT RES,DEPT MED CHEM POINTE CLAIRE H9R 4P8 PQCANADA
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 1, volume: 315, anno: 1994,
pagine: 111 - 118
SICI:
0003-9861(1994)315:1<111:PACORH>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROSTAGLANDIN ENDOPEROXIDE SYNTHASE; NONSTEROIDAL ANTIINFLAMMATORY DRUGS; INDUCIBLE CYCLOOXYGENASE; EXPRESSION; CELLS; SYNTHETASE; IDENTIFICATION; INACTIVATION; MECHANISM; ISOZYMES;
Keywords:
CYCLOOXYGENASE-2; PROSTAGLANDIN G/H SYNTHASE-2; RECOMBINANT; BACULOVIRUS; VACCINIA VIRUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
M.D. Percival et al., "PURIFICATION AND CHARACTERIZATION OF RECOMBINANT HUMAN CYCLOOXYGENASE-2", Archives of biochemistry and biophysics, 315(1), 1994, pp. 111-118

Abstract

Recombinant human cyclooxygenase-2 (hCox-2, Prostaglandin G/H synthase-2) has been purified from baculovirus-Sf9 and vaccina virus-Cos-7 cell expression systems. The detergent-solubilized, purified enzyme is heterogeneous in terms of its glycosylation. The vaccinia virus hCox-2 is a mixture of two glycoforms, whereas baculovirus hCox-2 comprises at least four species. The specific cyclooxygenase activities of both enzymes are 43 mu mol O-2/min/mg with arachidonic acid which is within the range of values reported for ovine Cox-1. The K-m values of arachidonic acid for hCox-2 and ovine Cox-1 are 0.9 and 2.7 mu M, respectively. Six other C-18 and C-20 fatty acids containing at least one 1,4-cis,cis-pentadiene moiety were also identified as substrates for hCox-2. Linoleic and gamma-linolenic acid were determined by mass spectrometry as being hydroxylated primarily at the C-9 and C-13 positions, whereas linolenic acid was hydroxylated primarily at the C-12 and C-16 positions. hCox-2 binds heme such that maximal activity is observed at a stoichiometry of 1.0 heme per enzyme subunit. The apparent molecular mass of hCox-2, determined by gel filtration chromatography in the presence of 2.0% beta-octylglucoside, is consistent with a dimeric structure. The results of this study indicate that the physical and catalytic properties of recombinant hCox-2 are very similar to that of the extensively studied ovine Cox-1. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 03:40:22