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Titolo:
Isolation and comparison of natural and recombinant human CENP-A autoantigen
Autore:
Martinez, A; Sun, DX; Billings, PB; Swiderek, KM; Sullivan, KF; Hoch, SO;
Indirizzi:
Agouron Inst, La Jolla, CA 92037 USA Agouron Inst La Jolla CA USA 92037Agouron Inst, La Jolla, CA 92037 USA City Hope Natl Med Ctr, Beckman Res Inst, Duarte, CA 91010 USA City Hope Natl Med Ctr Duarte CA USA 91010 Res Inst, Duarte, CA 91010 USA Scripps Clin & Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA
Titolo Testata:
JOURNAL OF AUTOIMMUNITY
fascicolo: 6, volume: 11, anno: 1998,
pagine: 611 - 619
SICI:
0896-8411(199812)11:6<611:IACONA>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
INNER KINETOCHORE PLATE; CENTROMERE PROTEIN; ANTICENTROMERE ANTIBODIES; MAMMALIAN CENTROMERE; SYSTEMIC-SCLEROSIS; HUMAN-CELLS; HISTONE; AUTOANTIBODIES; PERFORMANCE; SCLERODERMA;
Keywords:
anticentromere antibodies (ACA); human CENP-A; recombinant CENP-A; scleroderma; SSc;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Hoch, SO Agouron Inst, 505 Coast Blvd S, La Jolla, CA 92037 USA Agouron Inst 505 Coast Blvd S La Jolla CA USA 92037 CA 92037 USA
Citazione:
A. Martinez et al., "Isolation and comparison of natural and recombinant human CENP-A autoantigen", J AUTOIMMUN, 11(6), 1998, pp. 611-619

Abstract

Anticentromere antibodies (ACA) are associated with systemic sclerosis (scleroderma) patients exhibiting the more benign or so called limited manifestation of the disease (lSSc). ACA reactivity is directed against multiple polypeptide targets, the smallest of which is designated CENP-A. CENP-A is not an abundant cellular constituent; therefore to maximize recovery, we developed a protocol with a minimum of steps to isolate CENP-A from a human cell line. The trace cellular amount of this protein clearly dictated the production of its recombinant counterpart to facilitate determination of the role of the CENP-A antigen in scleroderma pathogenesis. Here we describe theeukaryotic expression of CENP-A cDNA using baculovirus-mediated infection of insect cells. The non-fusion recombinant protein spans the natural residues of the human CENP-A protein and rCENP-A followed the same chromotographic sequence for purification as did the natural source. The availability ofthe bona fide antigen provided a critical standard upon which to document authenticity of the recombinant polypeptide. The two forms of this antigen have been compared and shown to exhibit similar physical and antigenic properties. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 07:16:05