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Titolo:
Purification and characterization of the 26S proteasome from cultured rice(Oryza sativa) cells
Autore:
Yanagawa, Y; Ohhashi, A; Murakami, Y; Saeki, Y; Yokosawa, H; Tanaka, K; Hashimoto, J; Sato, T; Nakagawa, H;
Indirizzi:
Chiba Univ, Fac Hort, Dept Bioprod Sci, Matsudo, Chiba 2718510, Japan Chiba Univ Matsudo Chiba Japan 2718510 Sci, Matsudo, Chiba 2718510, Japan Japan Sci & Technol Corp, CREST, Chiyoda Ku, Tokyo 1010062, Japan Japan Sci & Technol Corp Tokyo Japan 1010062 da Ku, Tokyo 1010062, Japan Jikei Univ, Sch Med, Dept Biochem 2, Minato Ku, Tokyo 1058461, Japan JikeiUniv Tokyo Japan 1058461 iochem 2, Minato Ku, Tokyo 1058461, Japan Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biochem, Kita Ku, Sapporo, Hokkaido 0600812, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600812 oro, Hokkaido 0600812, Japan Tokyo Metropolitan Inst Med Sci, Bunkyo Ku, Tokyo 1138613, Japan Tokyo Metropolitan Inst Med Sci Tokyo Japan 1138613 Tokyo 1138613, Japan Natl Inst Agrobiol Resources, Tsukuba, Ibaraki 3058602, Japan Natl Inst Agrobiol Resources Tsukuba Ibaraki Japan 3058602 3058602, Japan
Titolo Testata:
PLANT SCIENCE
fascicolo: 1, volume: 149, anno: 1999,
pagine: 33 - 41
SICI:
0168-9452(19991112)149:1<33:PACOT2>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
TAT-BINDING PROTEIN; ORNITHINE DECARBOXYLASE; ARABIDOPSIS-THALIANA; MOLECULAR CHARACTERIZATION; REGULATORY PARTICLE; SPINACIA-OLERACEA; UBIQUITIN SYSTEM; 26-S PROTEASOME; GENE FAMILY; ALPHA-TYPE;
Keywords:
26S proteasome; 20S proteasome; rice (Oryza sativa L.);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Nakagawa, H Chiba Univ, Fac Hort, Dept Bioprod Sci, Matsudo, Chiba 2718510, Japan Chiba Univ Matsudo Chiba Japan 2718510 , Chiba 2718510, Japan
Citazione:
Y. Yanagawa et al., "Purification and characterization of the 26S proteasome from cultured rice(Oryza sativa) cells", PLANT SCI, 149(1), 1999, pp. 33-41

Abstract

The 26S proteasome was purified from cultured rice cells to near homogeneity by ultracentrifugation for 5 h at 85,000 x g, chromatography on Biogel A-1.5m, and glycerol density-gradient centrifugation analysis. The purified enzyme had two distinct forms, termed 36S alpha- and 26S beta-type proteasomes, with different electrophoretic mobilities by nondenaturing polyacrylamide gel electrophoresis. It consisted of multiple polypeptides with molecular masses of 25-35 and 42-120 kDa, which presumably corresponded to those of the 20S proteasome and an associated PA700 regulatory complex, respectively. The rice 26S proteasome resembled, but was not identical to, one from other sources in their subunit composition and immunochemical reactivity. Intriguingly, both rice and spinach 26S proteasomes could not degrade rat ornithine decarboxylase in the presence of antizyme and ATP, unlike the rat 26S proteasome, implying the existence of functional differences between mammalian and plant 26S proteasomes. (C) 1999 Published by Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 12:17:01