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Titolo:
SIALYLATED OLIGOSACCHARIDE-SPECIFIC PLANT LECTIN FROM JAPANESE ELDERBERRY (SAMBUCUS-SIEBOLDIANA) BARK TISSUE HAS A HOMOLOGOUS STRUCTURE TO TYPE-II RIBOSOME-INACTIVATING PROTEINS, RICIN AND ABRIN - CDNA CLONINGAND MOLECULAR MODELING STUDY
Autore:
KAKU H; TANAKA Y; TAZAKI K; MINAMI E; MIZUNO H; SHIBUYA N;
Indirizzi:
NATL INST AGROBIOL RESOURCES,DEPT CELL BIOL TSUKUBA IBARAKI 305 JAPAN NATL INST AGROBIOL RESOURCES,DEPT APPL PHYSIOL TSUKUBA IBARAKI 305 JAPAN NATL INST AGROBIOL RESOURCES,DEPT MOLEC BIOL TSUKUBA IBARAKI 305 JAPAN NATL INST FORESTRY & FOREST PROD RES INST KUKIZAKI IBARAKI 305 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 3, volume: 271, anno: 1996,
pagine: 1480 - 1485
SICI:
0021-9258(1996)271:3<1480:SOPLFJ>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; A-CHAIN; MAACKIA-AMURENSIS; NIGRA L; FLOW-CYTOMETRY; SIALIC-ACID; EXPRESSION; 2.5-A; LEUKOAGGLUTININ; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
H. Kaku et al., "SIALYLATED OLIGOSACCHARIDE-SPECIFIC PLANT LECTIN FROM JAPANESE ELDERBERRY (SAMBUCUS-SIEBOLDIANA) BARK TISSUE HAS A HOMOLOGOUS STRUCTURE TO TYPE-II RIBOSOME-INACTIVATING PROTEINS, RICIN AND ABRIN - CDNA CLONINGAND MOLECULAR MODELING STUDY", The Journal of biological chemistry, 271(3), 1996, pp. 1480-1485

Abstract

Bark lectins from the elderberry species belonging to the genus Sambucus have a unique carbohydrate binding specificity for sialylated glycoconjugates containing NeuAc(alpha 2-G)Gal/GalNAc sequence. To elucidate the structure of the elderberry lectin, a cDNA library was constructed from the mRNA isolated from the bark tissue of Japanese elderberry(Sambucus siebobdiana) with lambda gt11 phage and screened with anti-S. sieboldiana agglutinin (SSA) antibody, The nucleotide sequence of acDNA clone encoding full-length SSA (LecSSA1) showed the presence of an open reading frame with 1902 base pairs, which corresponded to 570 amino acid residues, This open reading frame encoded a signal peptide and a linker region (19 amino acid residues) between the two subunits of SSA, the hydrophobic (A-chain) and hydrophilic (B-chain) subunits, This indicates that SSA is synthesized as a preproprotein and post-translationally cleaved into two mature subunits, Homology searching as well as molecular modeling studies unexpectedly revealed that each subunit of SSA has a highly homologous structure to the galactose-specificlectin subunit and ribosome-inactivating subunit of plant toxic proteins such as ricin and abrin, indicating a close evolutionary relationship between these carbohydrate-binding proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:23:54