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Titolo:
ISOLATION, CDNA CLONING, BIOLOGICAL PROPERTIES, AND CARBOHYDRATE-BINDING SPECIFICITY OF SIEBOLDIN-B, A TYPE-II RIBOSOME-INACTIVATING PROTEIN FROM THE BARK OF JAPANESE ELDERBERRY (SAMBUCUS-SIEBOLDIANA)
Autore:
ROJO MA; YATO M; ISHIIMINAMI N; MINAMI E; KAKU H; CITORES L; GIRBES T; SHIBUYA N;
Indirizzi:
NATL INST AGROBIOL RESOURCES,DEPT BIOTECHNOL TSUKUBA IBARAKI 305 JAPAN NATL INST AGROBIOL RESOURCES,DEPT BIOTECHNOL TSUKUBA IBARAKI 305 JAPAN UNIV VALLADOLID,DEPT BIOQUIM & BIOL MOL E-47005 VALLADOLID SPAIN
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 2, volume: 340, anno: 1997,
pagine: 185 - 194
SICI:
0003-9861(1997)340:2<185:ICCBPA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; A-CHAIN; NIGRA L; LECTIN; RICIN; RNA; MECHANISM; SEQUENCE; MODECCIN; PLANTS;
Keywords:
RIBOSOME-INACTIVATING PROTEIN; SAMBUCUS; ELDERBERRY; CDNA; CARBOHYDRATE BINDING; SURFACE PLASMON RESONANCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M.A. Rojo et al., "ISOLATION, CDNA CLONING, BIOLOGICAL PROPERTIES, AND CARBOHYDRATE-BINDING SPECIFICITY OF SIEBOLDIN-B, A TYPE-II RIBOSOME-INACTIVATING PROTEIN FROM THE BARK OF JAPANESE ELDERBERRY (SAMBUCUS-SIEBOLDIANA)", Archives of biochemistry and biophysics, 340(2), 1997, pp. 185-194

Abstract

A type II ribosome-inactivating protein (RIP) was isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) and named sieboldin-b, Sieboldin-b is a heterodimeric protein consisting of 27- and33-kDa subunits and showed strong ribosome-inactivating activity in vitro but did not show in vivo toxicity. The amino acid sequence of sieboldin-b deduced from the structure of the cDNA showed that both subunits of sieboldin-b are encoded on a single precursor polypeptide. Sieboldin-b has a structure homologous with the Neu5Ac(alpha 2-6)Gal/GalNAc-specific bark lectin from S. sieboldiana (SSA) and also typical typeII RIPs such as ricin and abrin. Detailed analyses of carbohydrate binding properties of sieboldin-b revealed that sieboldin-b binds to Gal/GalNAc, similar to ricin/abrin, in spite of its highly homologous structure with SSA. The biological properties of these toxins/lectins arecompared, and the possible explanation for such diversity is discussed. (C) 1997 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:26:09