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Titolo:
EXPRESSION AND CHARACTERIZATION OF A CYTOTOXIC HUMAN-FROG CHIMERIC RIBONUCLEASE - POTENTIAL FOR CANCER-THERAPY
Autore:
NEWTON DL; XUE Y; BOQUE L; WLODAWER A; KUNG HF; RYBAK SM;
Indirizzi:
NCI,LAB BIOCHEM PHYSIOL,DIV BASIC SCI,FREDERICK CANC RES & DEV CTR FREDERICK MD 21702 NCI,LAB BIOCHEM PHYSIOL,DIV BASIC SCI,FREDERICK CANC RES & DEV CTR FREDERICK MD 21702 NCI,INTRAMURAL RES SUPPORT PROGRAM,SAIC FREDERICK,FREDERICK CANC RES & DEV CTR FREDERICK MD 21702 NCI,MACROMOL STRUCT LAB,FREDERICK CANC RES & DEV CTR,ABL,BASIC RES PROGRAM FREDERICK MD 21702
Titolo Testata:
Protein engineering
fascicolo: 4, volume: 10, anno: 1997,
pagine: 463 - 470
SICI:
0269-2139(1997)10:4<463:EACOAC>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
EOSINOPHIL-DERIVED NEUROTOXIN; BOVINE SEMINAL RIBONUCLEASE; PROTEIN-SYNTHESIS INHIBITION; P-30 PROTEIN; ANTITUMOR RIBONUCLEASE; ESCHERICHIA-COLI; HUMAN ANGIOGENIN; RNASE; SUPERFAMILY; HYBRID;
Keywords:
ANTITUMOR; GENE; RECOMBINANT; RIBONUCLEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
D.L. Newton et al., "EXPRESSION AND CHARACTERIZATION OF A CYTOTOXIC HUMAN-FROG CHIMERIC RIBONUCLEASE - POTENTIAL FOR CANCER-THERAPY", Protein engineering, 10(4), 1997, pp. 463-470

Abstract

Onconase is a cytotoxic ribonuclease with antitumor properties. A semisynthetic gene encoding the entire protein sequence was constructed by fusing oligonucleotides coding for the first 15 and last six of the 104 amino acid residues to a genomic clone that encoded the remaining amino acid residues. Additionally, the 15 N-terminal amino acid residues of onconase were replaced with the first 21 amino acid residues of the homologous human RNase, eosinophil-derived neurotoxin, EDN. Two versions of the hybrid EDN-onconase protein were cloned, expressed and purified. The chimera that contained a glycine in lieu of the aspartic acid present in native onconase (position 26 in the chimera) exhibitedenzymatic activity more characteristic of EDN than native onconase and was considerably more active with respect to both RNase activity andcellular cytotoxicity than recombinant onconase. In contrast to native or recombinant onconase, the EDN chimera was recognized by anti-EDN polyclonal antibodies, demonstrating that the chimera also shared structural antigenic determinants to the human enzyme. These results demonstrate that a chimeric ribonuclease has cytotoxicity comparable to onconase in two out of four cell lines tested. The implications with regard to cancer therapy are presented.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 16:00:47