Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amp...Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amplification of cDNA Ends(RACE) technique, full-length cDNA and DNA sequences of ghrelin gene were obtained. The full-length ghrelin cDNA(GenBank accession no. JX122807) was 552 bp long, containing a 115 bp 5'-untranslated region, a 324 bp open reading frame and a 113 bp 3'-untranslated region. The full-length ghrelin DNA was 1 323 bp, consisting of three introns and four exons. The exon/intron junction sequences conformed to the GT/AG rule. Three introns were 594, 84 and 93 bp in length, respectively; four exons were229, 78, 112 and 133 bp in length, respectively. The results of amino acid sequence analysis showed that the deduced propreghrelin sequence of M. albus contained a signal peptide(SP) consisting of 22 amino acid residues, a mature peptide(MP)consisting of 19 amino acid residues and a C-terminal amino acid residue. Among them, the third amino acid of MP was serine(Ser^3) as the site for N-acylation and N-deacetylation reactions; the C-terminal amino acid residue sequence might contain a peptide hormone obestatin, which is a physiological antagonist of mature Ghrelin peptide. The homology and phylogenic relationships analyses of amino acid sequences suggested that propreghrelin of M. albus had high similarity to those of several Perciformes fishes; the propreghrelins of M. albus, Perciformes and Heterosomata fishes were clustered into a subgroup. The high conservatism of the gene structure and the amino acid sequences indicated that Ghrelin exerts important physiological functions and plays similar physiological mechanisms in vertebrates.展开更多
In this paper, in order to predict the residual deformation of thick spherical structure, a welding program is compiled in APDL language based on Ansys and a numerical welding experiment of a welding example is carrie...In this paper, in order to predict the residual deformation of thick spherical structure, a welding program is compiled in APDL language based on Ansys and a numerical welding experiment of a welding example is carried out. The temperature field of welding was simulated firstly, then a thermal-structure coupling analysis was carried out, and at last the residual stress and deformation after welding were got. After that, the numerical experiment result was compared with physical experiment one. The comparative analysis shows that the numerical simulation fits well with physical experiment. On the basis of that, a three-dimensional numerical experiment of a thick spherical shell structure was carried out to get the changing rule of stress and deformation of a thick spherical shell structure during welding. The research is of great value to the prediction of residual deformation and high precision machining.展开更多
The total RNA was extracted from Microtusfortis liver tissue which before being infected and after being infected 10 d and 15 d by the Schistosoma japonicum cercariae. Using Rattus norvegicus CD36 gene probe to hybrid...The total RNA was extracted from Microtusfortis liver tissue which before being infected and after being infected 10 d and 15 d by the Schistosoma japonicum cercariae. Using Rattus norvegicus CD36 gene probe to hybridize analysis of CD36 difference expression in the Microtus fortis liver tissues which were infected with Schistosorna japonicum before and after being infected. At the same time, the cDNA sequence and encoded amino acid sequence of the Rattus norvegicus CD36 gene and CD36 protein structural domains were analysized by using bioinformatics. The results showed that the CD36 expression levels in the liver tissue of Microtus fortis after being infected were significantly higher than before being infectied. The Rattus norvegicus CD36 cDNA sequence of a total length is 1625 bp and encoded 472 amino acid residues and Rattus norvegicus CD36 protein containing a CD36 superfamily domain.展开更多
基金Supported by Natural Science Foundation of Hubei Province(2013CFB393)Open Fund of Key Laboratory of Freshwater Fisheries and Germplasm Resources Utilizations,Ministry of Agriculture(KF201307)+2 种基金National Pillar Program of China(2013BAD20B06)Pillar Program of Hubei Province(2015BBA235)Program for Outstanding Young and Middle-aged Scientific Innovation Team in Colleges and Universities of Hubei Province(T201503)
文摘Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amplification of cDNA Ends(RACE) technique, full-length cDNA and DNA sequences of ghrelin gene were obtained. The full-length ghrelin cDNA(GenBank accession no. JX122807) was 552 bp long, containing a 115 bp 5'-untranslated region, a 324 bp open reading frame and a 113 bp 3'-untranslated region. The full-length ghrelin DNA was 1 323 bp, consisting of three introns and four exons. The exon/intron junction sequences conformed to the GT/AG rule. Three introns were 594, 84 and 93 bp in length, respectively; four exons were229, 78, 112 and 133 bp in length, respectively. The results of amino acid sequence analysis showed that the deduced propreghrelin sequence of M. albus contained a signal peptide(SP) consisting of 22 amino acid residues, a mature peptide(MP)consisting of 19 amino acid residues and a C-terminal amino acid residue. Among them, the third amino acid of MP was serine(Ser^3) as the site for N-acylation and N-deacetylation reactions; the C-terminal amino acid residue sequence might contain a peptide hormone obestatin, which is a physiological antagonist of mature Ghrelin peptide. The homology and phylogenic relationships analyses of amino acid sequences suggested that propreghrelin of M. albus had high similarity to those of several Perciformes fishes; the propreghrelins of M. albus, Perciformes and Heterosomata fishes were clustered into a subgroup. The high conservatism of the gene structure and the amino acid sequences indicated that Ghrelin exerts important physiological functions and plays similar physiological mechanisms in vertebrates.
文摘In this paper, in order to predict the residual deformation of thick spherical structure, a welding program is compiled in APDL language based on Ansys and a numerical welding experiment of a welding example is carried out. The temperature field of welding was simulated firstly, then a thermal-structure coupling analysis was carried out, and at last the residual stress and deformation after welding were got. After that, the numerical experiment result was compared with physical experiment one. The comparative analysis shows that the numerical simulation fits well with physical experiment. On the basis of that, a three-dimensional numerical experiment of a thick spherical shell structure was carried out to get the changing rule of stress and deformation of a thick spherical shell structure during welding. The research is of great value to the prediction of residual deformation and high precision machining.
文摘The total RNA was extracted from Microtusfortis liver tissue which before being infected and after being infected 10 d and 15 d by the Schistosoma japonicum cercariae. Using Rattus norvegicus CD36 gene probe to hybridize analysis of CD36 difference expression in the Microtus fortis liver tissues which were infected with Schistosorna japonicum before and after being infected. At the same time, the cDNA sequence and encoded amino acid sequence of the Rattus norvegicus CD36 gene and CD36 protein structural domains were analysized by using bioinformatics. The results showed that the CD36 expression levels in the liver tissue of Microtus fortis after being infected were significantly higher than before being infectied. The Rattus norvegicus CD36 cDNA sequence of a total length is 1625 bp and encoded 472 amino acid residues and Rattus norvegicus CD36 protein containing a CD36 superfamily domain.
