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Titolo:
Single-step method for purification of Shiga toxin-1 B subunit using receptor-mediated affinity chromatography by globotriaosylceramide-conjugated octyl sepharose CL-4B
Autore:
Nakajima, H; Katagiri, YU; Kiyokawa, N; Taguchi, T; Suzuki, T; Sekino, T; Mimori, K; Saito, M; Nakao, H; Takeda, T; Fujimoto, J;
Indirizzi:
Natl Childrens Med Res Ctr, Dept Pathol, Setagaya Ku, Tokyo 1548509, JapanNatl Childrens Med Res Ctr Tokyo Japan 1548509 Ku, Tokyo 1548509, Japan Natl Childrens Med Res Ctr, Dept Infect Dis Res, Setagaya Ku, Tokyo 1548509, Japan Natl Childrens Med Res Ctr Tokyo Japan 1548509 Ku, Tokyo 1548509, Japan Japan Sci & Technol Corp, Kawaguchi, Saitama 3320012, Japan Japan Sci & Technol Corp Kawaguchi Saitama Japan 3320012 a 3320012, Japan
Titolo Testata:
PROTEIN EXPRESSION AND PURIFICATION
fascicolo: 2, volume: 22, anno: 2001,
pagine: 267 - 275
SICI:
1046-5928(200107)22:2<267:SMFPOS>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEMOLYTIC-UREMIC SYNDROME; BURKITTS-LYMPHOMA CELLS; FATTY-ACID CONTENT; ESCHERICHIA-COLI; GLYCOLIPID RECEPTOR; VEROTOXIN BINDING; ENDOTHELIAL-CELLS; CRYSTAL-STRUCTURE; APOPTOSIS; CERAMIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Fujimoto, J Natl Childrens Med Res Ctr, Dept Pathol, Setagaya Ku, 3-35-1 Taishido, Tokyo 1548509, Japan Natl Childrens Med Res Ctr 3-35-1 Taishido Tokyo Japan 1548509
Citazione:
H. Nakajima et al., "Single-step method for purification of Shiga toxin-1 B subunit using receptor-mediated affinity chromatography by globotriaosylceramide-conjugated octyl sepharose CL-4B", PROT EX PUR, 22(2), 2001, pp. 267-275

Abstract

A new single-step purification method for Shiga toxin (Stx) was developed using receptor-mediated affinity chromatography, in which Gb3Cer (globotriaosylceramide) was conjugated to octyl Sepharose CL-4B as a carrier This method achieves high yield and high purity in a small column on which Gb3Cer has been immobilized at high density. Using this affinity column, the Stx1 Bsubunit was purified with homogeneity by a one-step procedure from a crudeextract of recombinant Stx1 B subunit-producing Escherichia coli. The purified Stx1 B subunit conserved a natural pentamer structure confirmed by gelfiltration and sedimentation equilibrium analysis. Furthermore, the purified Stx1 B subunit was able to bind specifically to Gb3Cer expressed on Burkitt's lymphoma cells. This versatile purification method can be used to isolate various types of natural as well as recombinant Stx, facilitating fundamental studies of human diseases caused by this toxin. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/20 alle ore 22:07:54