38 resultados para Receptor activator of nuclear factor
Resumo:
A specific activator of blood coagulation factor X was purified from the venom of Bungarus fasciatus by gel filtration and by ion-exchange chromatography on a Mono-Q column (FPLC). It consisted of a single polypeptide chain, with a mel. wt of 70,000 in reducing and non-reducing conditions. The enzyme had an amidolytic activity towards the chromogenic substrates S-2266 and S-2302 but it did not hydrolyse S-2238, S2251 or S-2222, which are specific substrates for thrombin, plasmin and factor Xa, respectively. The enzyme activated factor X in vitro and the effect was Ca2+ dependent with a Hill coefficient of 7.9. As with physiological activators, the venom activator cleaves the heavy chain of factor X, producing the activated factor Xa alpha. The purified factor X activator from B. fasciatus venom did not activate prothrombin, nor did it cleave or clot purified fibrinogen. The amidolytic activity and the factor X activation activity of the factor X activator from B. fasciatus venom were readily inhibited by serine protease inhibitors such as diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), benzamidine and by soybean trypsin inhibitor but not by EDTA. These observations suggest that the factor X activator from B. fasciatus venom is a serine protease. It therefore differs from those of activators obtained from Vipera russelli and Bothrops atrox venoms, which are metalloproteinases.
Resumo:
DNAnrDNAnrDNAITS5S-NTS5S rDNAITS 1 nrDNA ITS1 ;2ITS1;3ITS1;45S rDNA 1. ITSITS1 ITS1 944-3271 bp, ITS;2 ITS295-GGCCACCCTAGTC LSRSSR;3 ITS1; 4 ITS1GC 2. ITS1ITS11MLMP; 2 SSR9SSR;3SSRnrDNA ITS ;4LSR SSR 3. ITS1 Mfold 3.2 11ITS15631 ITS1;2 ;35-GGCCACCCTAGTC 4. 5S rDNA 35S rDNA 45 1 5S rDNA120 bp, GGG CTC;2 5S rDNA90-99%; 3poly-Cpoly-TTCGC5S rDNAType A 751-764 bpType B 770-807 bp 32 bpType C 581-594 bp; 5Type AType B 148-175 bpType C 143 bp56.0-66.8% 5. 5S rRNA Mfold 3.2 15S rRNA5-2CD3B1B2 E1A, ;2 ;35I IV
Resumo:
The pantherine lineage of the cat family Felidae (order: Carnivora) includes five big cats of genus Panthera and a great many midsized cats known worldwide. Presumably because of their recent and rapid radiation, the evolutionary relationship among pantherines remains ambiguous. We provide an independent assessment of the evolutionary history of pantherine lineage using two complete mitochondrial (mt) genes (ND2 and ND4) and the nuclear beta-fibrmogen intron 7 gene, whose utility in carnivoran phylogeny was first explored. The available four mt (ND5, cytb, 12S, and 16SrRNA) and two nuclear (IRBP and TTR) sequence loci were also combined to reconstruct phylogeny of 14 closely related cat species. Our analyses of combined mt data (six genes; approximate to 3750 bp) and combined mt and nuclear data (nine genes; approximate to 6500 bp) obtained identical tree topologies, which were well-resolved and strongly supported for almost all nodes. Monophyly of Panthera genus in pantherine lineage was confirmed and interspecific affinities within this genus revealed a novel branching pattern, with P. tigris diverging first in Panthera genus, followed by P. onca, P. leo, and last two sister species P. pardus and P. uncia. In addition, close association of Neofelis nebulosa to Panthera, the phylogenetic redefinition of Otocolobus manil within the domestic cat group, and the relatedness of Acinonyx jubatus and Puma concolor were all important findings in the resulting phylogenies. The potential utilities of nine different genes for phylogenetic resolution of closely related pantherine species were also evaluated, with special interest in that of the novel nuclear beta-fibrinogen intron 7. (c) 2005 Elsevier Inc. All rights reserved.
Resumo:
Euglena gracilis cell was extracted sequentially with CSK-Triton buffer, RSB-Magik solution and DNase-As solution. DGD embedment-free electron microscopy showed that in the extracted nucleus there was a residual non-chromatin fibrous network. That it could not be removed by hot trichloroacetic acid further supported the idea that it was a non-histone, non-chromatin fibrous protein network, and should be the internal network of the nuclear matrix. After the sequential extraction, the nuclear membrane was removed, leaving behind a layer of lamina; the chromatin was digested and eluted from the dense chromosomes and residual chromosomal structures that should be chromosomal scaffold were revealed. Western blot analysis with antiserum against rat lamins showed that nuclear lamina of the cell possessed two positive polypeptides, a major one and a minor one, which had molecular masses similar to lamin B and lamin A, respectively. Comparing these data with those of the most primitive eukaryote Archezoa and of higher eukaryotes, it was suggested that the lower unicellular eukaryote E. gracillis already had the nuclear matrix structure, and its nuclear matrix (especially the lamina) might represent a stage of evolutionary history of the nuclear matrix. (C) 2000 Editions scientifiques et medicales Elsevier SAS.
Resumo:
The enhancement of quality factor for TE whispering-gallery modes is analyzed for three-dimensional microcylinder resonators based on the destructive interference between vertical leakage modes. In the microcylinder resonator, the TE whispering-gallery modes can couple with vertical propagation modes, which results in vertical radiation loss and low quality factors. However, the vertical loss can be canceled by choosing appropriate thickness of the upper cladding layer or radius of the microcylinder. A mode quality factor increase by three orders of magnitude is predicted by finite-difference time-domain simulation. Furthermore, the condition of vertical leakage cancellation is analyzed.
Resumo:
The magnetic field dependence of filling factors has been investigated on InP based In-0.53 Ga0.47As/In-0.52 Al-0.48 As quantum well samples with two occupied subbands by means of magnetotransport measurements at the temperature of 1.5 K in a magnetic field range of 0 to 13 T. Under the condiction that Laundau-level broadening is larger than the spin splitting of each subband, filling factors are even when the splitting energy of two subbands is an integer multiple of the cyclotron energy, i. e. Delta E-21 = khw(c). If the splitting energy of two subbands is half of an odd interger multiple of the cyclotron erergy, i. e. Delta E-21 = (2 k + 1) hw(c) /2, the filling factor is odd.
