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	Provedor de dados OAK (1) J. Venom. Anim. Toxins incl. Trop. Dis. (1) Autor Chen,J (1) Fukuda, K (1) Ishii, T (1) Morita, M (1) Senda, A (1) Terabayashi, T (1) Urashima, T (1) Wei,CB (1) 浦島, 匡 (1) 福田, 健二 (1) Mais... Palavra-chave Lipocalin (2) CDNA library (1) Colostrum (1) Deinagkistrodon acutus (1) Gene expression pattern analysis (1) Odorant-binding protein (1) Pheromone transport (1) Phylogeny (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Ano 2012 (1) 2009 (1) País Brazil (1) Japan (1) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última A novel lipocalin homologue from the venom gland of Deinagkistrodon acutus similar to mammalian lipocalins J. Venom. Anim. Toxins incl. Trop. Dis. Wei,CB; Chen,J. Lipocalins are involved in a variety of functions including retinol transport, cryptic coloration, olfaction, pheromone transport, prostaglandin synthesis, regulation of the immune response and cell homeostatic mediation. A full-length cDNA clone (named d-lipo), isolated from the venom gland cDNA library of Deinagkistrodon acutus, contained an insert of 664 bp including an open reading frame that encodes a lipocalin homologue of 177 amino acids. Comparison of d-lipo and other related proteins revealed an overall amino acid identity of less than 21.5%. Primary structures of d-lipo carried three structurally conserved regions (SCR) showing homologies to those of lipocalins. The first conserved Cys residue - the essential amino acid residue for the catalytic... Tipo: Info:eu-repo/semantics/article Palavras-chave: Deinagkistrodon acutus; CDNA library; Lipocalin; Phylogeny; Gene expression pattern analysis. Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000100003 Short communication : Evidence for the presence of a putative odorant-binding protein in bovine colostrum OAK Fukuda, K; Senda, A; Ishii, T; Urashima, T; Morita, M; Terabayashi, T; 福田, 健二; 浦島, 匡. Using a combination of PAGE and mass spectrom etry for protein identification，we obtained evidence that a putative odorant-binding protein，designated hypothetical protein LOC517854，occurs in bovine colostrum. This protein，termed as a putative bovine colostral odorant-binding protein (bcOBP)， consists of 172 AA residues，including a putative 16-AA signal peptide. The theoreticalis oelectric point value and molecular mass of the full-length sequence of bcOBP were calculated to be 4.57 and 19604.18，respectively. The highest sequence similarity (83%) was observed with a potential pheromone transporter，Allergen Bos d 2. An odorant-binding protein derived from bovine nasal mucosa showed relatively low sequence similarity(52%) against bcOBP. Its biological... Palavras-chave: Colostrum; Lipocalin; Odorant-binding protein; Pheromone transport. Ano: 2009 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/2674 Registros recuperados: 2 Primeira ... 1 ... Última

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