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Titolo:
Isolation, characterization and molecular cloning of beta-D-glucan exohydrolase from cultured tobacco cells
Autore:
Koizumi, N; Okushima, Y; Sano, H;
Indirizzi:
Nara Inst Sci & Technol, Nara 6300101, Japan Nara Inst Sci & Technol Nara Japan 6300101 Technol, Nara 6300101, Japan
Titolo Testata:
JOURNAL OF PLANT PHYSIOLOGY
fascicolo: 6, volume: 157, anno: 2000,
pagine: 691 - 698
SICI:
0176-1617(200012)157:6<691:ICAMCO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
HOST-PATHOGEN INTERACTIONS; BARLEY HORDEUM-VULGARE; SOYBEAN CELLS; D-GLUCOSIDASE; HIGHER-PLANTS; L SEEDLINGS; CDNA CLONE; PURIFICATION; WALLS; BETA-1,3-GLUCANASE;
Keywords:
4-NPG 4-nitrophenyl beta-D-glucoside; PCR polymerase chain reaction; SDS-PAGE SDS-polyacrylamide gel electrophoresis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Koizumi, N Nara Inst Sci & Technol, 8916-5 Takayama Cho, Nara 6300101, Japan Nara Inst Sci & Technol 8916-5 Takayama Cho Nara Japan 6300101
Citazione:
N. Koizumi et al., "Isolation, characterization and molecular cloning of beta-D-glucan exohydrolase from cultured tobacco cells", J PLANT PHY, 157(6), 2000, pp. 691-698

Abstract

We purified an abundant cationic 68 kDa protein from the culture medium oftobacco BY2 (Nicotiana tabacum L. cv. Bright Yellow 2) cells and determined the amino acid sequence of its N-terminus and some internal peptides. Similar sequences were found in barley beta -D-glucan exohydrolase [EC 3.2.1.73], and the purified 68 kDa protein had beta -glucosidase activity. The purified protein released glucose from a mixture of laminaridextrins (beta -1,3-oligoglucosides). In addition to beta -1,3-linkages, the enzyme also hydrolyzed beta -1,4- and beta -1,6-linkages of glucose. A cDNA encoding tobacco beta -D-glucan exohydrolase was isolated using polymerase chain reaction (PCR) based on the internal amino acid sequence. The deduced amino acid sequence of tobacco beta -glucan exohydrolase showed 73 %, 74% and 44% amino acid identity with barley beta -D-glucan exohydrolase, nasturtium beta -D-glucosidase and 1,4-beta -D-glucan glucohydrolase D (CELD) of Pseudomonas fluorescens, respectively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 19:35:22