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Titolo:
EFFECT OF PEGYLATION ON THE STRUCTURE AND FUNCTION OF HORSE CYTOCHROME-C
Autore:
MABROUK PA;
Indirizzi:
NORTHEASTERN UNIV,DEPT CHEM BOSTON MA 02115
Titolo Testata:
Bioconjugate chemistry
fascicolo: 3, volume: 5, anno: 1994,
pagine: 236 - 241
SICI:
1043-1802(1994)5:3<236:EOPOTS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
BIS(4-PYRIDYL)DISULFIDE-MODIFIED GOLD ELECTRODE; RESONANCE RAMAN-SPECTRA; ORGANIC-SOLVENTS; POLYETHYLENE-GLYCOL; HEME-PROTEINS; TEMPERATURE-DEPENDENCE; CHEMICAL MODIFICATION; COVALENT ATTACHMENT; ENZYMATIC CATALYSIS; BINDING ABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
P.A. Mabrouk, "EFFECT OF PEGYLATION ON THE STRUCTURE AND FUNCTION OF HORSE CYTOCHROME-C", Bioconjugate chemistry, 5(3), 1994, pp. 236-241

Abstract

The preparation and spectrophotometric characterization of (both Fe2and Fe3+ forms) poly(ethylene glycol) (PEG; av FW 5000)-modified horse cytochrome c (cyt c(PEG)n) with different degrees of modification (n(av) = 6, 19) by UV-vis spectroscopy, circular dichroism spectroscopy,resonance Raman spectroscopy, and cyclic voltammetry are described. Extensive modification (n(av) = 19) of cyt c causes gross structural deformation of the heme as evidenced by major spectral changes in the UV-vis and circular dichroism spectral signatures of both the Fe2+ and Fe3+ forms. Modification of cyt c by six PEG residues, however, produces a protein in which the heme active site is structurally and functionally intact (UV-vis, circular dichroism, and resonance Raman) and which exhibits at least quasireversible direct electron transfer (E-degrees' = 338 +/- 5 mV vs SHE; (2.1 +/- 0.6) x 10(-3) cm/s) at bis(4-pyridyl) disulfide-modified Au electrodes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 04:34:37