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Titolo:
Molecular cloning and sequence analysis of stearoyl-CoA desaturase in milkfish, Chanos chanos
Autore:
Hsieh, SL; Liao, WL; Kuo, CM;
Indirizzi:
Natl Pingtung Univ Sci & Technol, Dept Aquaculture, Pingtung 912, Taiwan Natl Pingtung Univ Sci & Technol Pingtung Taiwan 912 ingtung 912, Taiwan Natl Taiwan Univ, Inst Fisheries Sci, Taipei 106, Taiwan Natl Taiwan UnivTaipei Taiwan 106 nst Fisheries Sci, Taipei 106, Taiwan
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 4, volume: 130, anno: 2001,
pagine: 467 - 477
SICI:
1096-4959(200112)130:4<467:MCASAO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
FATTY-ACID DESATURASE; INDUCED GENE-EXPRESSION; MOUSE-LIVER; 3T3-L1 PREADIPOCYTES; MESSENGER-RNA; SINGLE-GENE; DELTA-9; CARP; DELTA(9)-DESATURASE; ENZYME;
Keywords:
stearoyl-CoA desaturase; cDNA; milkfish; rapid amplification of cDNA ends (RACE); expression; polymerase chain-reaction (PCR); histidine motifs; phylogenetic relationship;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Kuo, CM Natl Pingtung Univ Sci & Technol, Dept Aquaculture, Pingtung 912, Taiwan Natl Pingtung Univ Sci & Technol Pingtung Taiwan 912 912, Taiwan
Citazione:
S.L. Hsieh et al., "Molecular cloning and sequence analysis of stearoyl-CoA desaturase in milkfish, Chanos chanos", COMP BIOC B, 130(4), 2001, pp. 467-477

Abstract

Stearoyl-CoA desaturase (EC 1.14.99.5) is a key enzyme in the biosynthesisof polyunsaturated fatty acids and the maintenance of the homeoviscous fluidity of biological membranes. The stearoyl-CoA desaturase cDNA in milkfishChanos chanos) was cloned by RT-PCR and RACE, and it was compared with thestearoyl-CoA desaturase in cold-tolerant teleosts, common carp and grass carp. Nucleotide sequence analysis revealed that the cDNA clone has a 972-bpopen reading frame encoding 323 amino acid residues. Alignments of the deduced amino acid sequence showed that the milkfish stearoyl-CoA desaturase shares 79% and 75% identity with common carp and grass carp, and 63%-64% with other vertebrates such as sheep, hamsters, rats, mice, and humans. Like common carp and grass carp, the deduced amino acid sequence in milkfish wellconserves three histidine cluster motifs (one HXXXXH and two HXXHH) that are essential for catalysis of stearoyl-CoA desaturase activity. However, RT-PCR analysis showed that stearoyl-CoA desaturase expression in milkfish isdetected in the tissues of liver, muscle, kidney, brain, and gill, and more expression sites were found in milkfish than in common carp and grass carp. Phylogenic relationships among the deduced stearoyl-CoA desaturase aminoacid sequence in milkfish and those in other vertebrates showed that the milkfish stearoyl-CoA desaturase amino acid sequence is phylogenetically closer to those of common carp and grass carp than to other higher vertebrates. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 07:12:51