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Titolo:
Characterization of acyl-CoA-binding protein (ACBP) in the pheromone glandof the silkworm, Bombyx mori
Autore:
Matsumoto, S; Yoshiga, T; Yokoyama, N; Iwanaga, M; Koshiba, S; Kigawa, T; Hirota, H; Yokoyama, S; Okano, K; Mita, K; Shimada, T; Tatsuki, S;
Indirizzi:
RIKEN, Inst Phys & Chem Res, Wako, Saitama 3510198, Japan RIKEN Wako Saitama Japan 3510198 & Chem Res, Wako, Saitama 3510198, Japan Univ Tokyo, Grad Sch Agr & Life Sci, Dept Agr & Environm Biol, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Agr & Environm Biol, Tokyo 1138657, Japan Natl Inst Radiol Sci, Genome Res Grp, Chiba 2638555, Japan Natl Inst Radiol Sci Chiba Japan 2638555 e Res Grp, Chiba 2638555, Japan
Titolo Testata:
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
fascicolo: 6-7, volume: 31, anno: 2001,
pagine: 603 - 609
SICI:
0965-1748(20010427)31:6-7<603:COAP(I>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
BIOSYNTHESIS ACTIVATING NEUROPEPTIDE; INTRACELLULAR SIGNAL-TRANSDUCTION; SEX-PHEROMONE; 3-DIMENSIONAL STRUCTURE; LEPIDOPTERAN INSECTS; MANDUCA-SEXTA; BOVINE LIVER; PBAN ACTION; COENZYME-A; INVOLVEMENT;
Keywords:
Bombyx mori; pheromone gland; acyl-CoA-binding protein; PBAN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Matsumoto, S RIKEN, Inst Phys & Chem Res, Hirosawa 2-1, Wako, Saitama 3510198, Japan RIKEN Hirosawa 2-1 Wako Saitama Japan 3510198 3510198, Japan
Citazione:
S. Matsumoto et al., "Characterization of acyl-CoA-binding protein (ACBP) in the pheromone glandof the silkworm, Bombyx mori", INSEC BIO M, 31(6-7), 2001, pp. 603-609

Abstract

Various fatty acyl-CoAs are involved as intermediates or precursors of sexpheromone components in the biosynthetic pathway of the pheromones in manylepidopteran insects. We have purified a 10-kDa protein from the cytosolicfraction of Bombyx mori pheromone glands by using affinity chromatography with a palmitoyl-CoA-agarose column and reversed-phase HPLC. Amino acid sequence analysis of the fragment peptides obtained from the purified protein,and a homology search, revealed that this protein was a member of acyl-CoA-binding proteins (ACBPs). MALDI-TOF mass spectral analysis of the purifiedprotein and cloning of the gene from a pheromone gland cDNA library confirmed B. mori ACBP to be a 90 amino acid protein with 78.9% identity to that of Manduca sexta ACBP. The secondary structure of the recombinant B. mori ACBP was determined by NMR spectroscopy. Northern blot analysis demonstratedthat B. mori ACBP was predominantly expressed in the pheromone gland and the corresponding transcript was expressed from the day before adult eclosion. Present results suggest that ACBP plays a significant role in the production of sex pheromones regulated by the neurohormone. pheromone biosynthesis activating neuropeptide (PBAN). (C) 2001 Elsevier Science Ltd. All rightsreserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 06:55:54