Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PREPARATION OF AN ACTIVITY-INHIBITING MONOCLONAL-ANTIBODY AGAINST HUMAN PLACENTAL AROMATASE CYTOCHROME-P450
Autore:
WASHIDA N; KITAWAKI J; HIGASHIYAMA T; MATSUI S; OSAWA Y;
Indirizzi:
HAUPTMAN WOODWARD MED RES INST INC,ENDOCRINE BIOCHEM DEPT,73 HIGH ST BUFFALO NY 14203 HAUPTMAN WOODWARD MED RES INST INC,ENDOCRINE BIOCHEM DEPT BUFFALO NY 14203 ROSWELL PK CANC INST BUFFALO NY 14263
Titolo Testata:
Steroids
fascicolo: 3, volume: 61, anno: 1996,
pagine: 126 - 132
SICI:
0039-128X(1996)61:3<126:POAAMA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
AFFINITY-CHROMATOGRAPHY; PURIFICATION; AROMATIZATION;
Keywords:
AROMATASE; MONOCLONAL ANTIBODY; ESTROGEN BIOSYNTHESIS; CYTOCHROME P450;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
N. Washida et al., "PREPARATION OF AN ACTIVITY-INHIBITING MONOCLONAL-ANTIBODY AGAINST HUMAN PLACENTAL AROMATASE CYTOCHROME-P450", Steroids, 61(3), 1996, pp. 126-132

Abstract

We produced a murine monoclonal antibody (MAb) to human placental aromatase cytochrome P450. This MAb, designated MAb3-2C2, was selected onits ability to suppress aromatase activity. Tile specificity of this MAb was assessed by selective immunoprecipitation of I-125-labeled aromatase cytochrome P450 as well as by the identification of a 55-kDa protein, which was enriched and purified by immunoaffinity chromatography on a MAb-coupled Sepharose 4B column. The MAb was able to suppress both human placental and ovarian microsomal aromatase. Species differences of aromatase were recognized by MAb3-2C2 on the basis of differential imununosuppression of aromatase activity. The antibody had no effect on non-aromatase cytochrome P450s. MAb3-2C2 gave negative results with human placental aromatase P450 in the Western blot analysis. The data presented indicate that MAb3-2C2 is specific fbi aromatase cytochrome P450 and that its epitope is located in a fragile tertiary conformation of the enzyme, thus making it capable of sensitively affecting catalysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 02:01:32