280马力。电喷1500转65码配457桥十档箱，请问想让快一点可以吗？_百度知道
280马力。电喷1500转65码配457桥十档箱，请问想让快一点可以吗？
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系统奖励20（财富值+经验值）+难题奖励20（财富值+经验值）
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可以的。如果你要改桥可以换成斯太尔的
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出门在外也不愁Early oral feeding in acute pancreatitis: an alternative approach to tube feeding. Preliminary report.
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2006 Mar-A106(2):181-6.Early oral feeding in acute pancreatitis: an alternative approach to tube feeding. Preliminary report.1, , , .1Clinical Hospital "Gailezers", Department of Surgery, Riga, Latvia. pupelis@gailes.lvAbstractINTRODUCTION: Jejunal feeding is accepted in the treatment of severe acute pancreatitis (AP). Early oral feeding (EOF) is deemed to be detrimental in the early phase of AP. The aim of this study was to assess the safety and effectiveness of EOF in the treatment of AP.MATERIALS AND METHODS: 29 AP patients were prospectively enrolled within 1.96 days from the onset of disease. APACHE II score, SIRS, MODS, serum CRP and lipase were evaluated. All patients received EOF when gastro-enteric transit was not severely impaired. ICU, hospital stay and main outcomes were assessed.RESULTS: APACHE II score was & or = 8 in 10 patients at the admission ranging 0-13 points for the whole group. Alcohol (62%) and gallstones (38%) were the main etiologic factors. SIRS and MODS were diagnosed in 65% and pleural effusion in 24% of patients. EOF was started on average 3.27 days after admission providing 571 ml (280.0-1115.0 ml) of enteral formula daily for 10.38 days. Median lipase activity was 690 U/l (90-10175 U/l) and CRP concentration reached 91.25 mg/dL (3.5-210 mg/dL) before EOF. Progressive decrease of lipase activity and CRP concentration was observed during the EOF course, reaching median CRP 18.6 mg/L (4.6-96.7mg/L) by discharge. Two patients underwent surgical intervention. Minor side effects of EOF were successfully managed in 4 patients. No mortality was observed.CONCLUSION: EOF could be a safe and effective alternative of nutritional support in AP patients when gastro-enteric transit is not severely impaired. For better EOF assessment further clinical trials are required.PMID:
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External link. Please review our .3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Esc...
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1978 Jun 25;253(12):4259-65.3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli., , .AbstractThe phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate phosphorylating), EC 4.2.1.15) was purified to apparent homogeneity from extracts of Escherichia coli K12. The enzyme has a molecular weight of 140,000 as judged by gel filtration and sedimentation equilibrium analysis. The enzyme has a subunit molecular weight of 35,000 as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, suggesting that the native form of the enzyme is a tetramer. This was confirmed by cross-linking the enzyme with dimethylsuberimidate and by analyzing the cross-linked material by gel electrophoresis in the presence of sodium dodecyl sulfate. The enzyme shows a narrow pH optimum between pH 6.5 and 7.0. The enzyme is stable for several months when stored at -20 degrees C in buffers containing phosphoenolpyruvate. Removal of phosphoenolpyruvate causes an irreversible inactivation of the enzyme. The enzyme is strongly inhibited by L-phenylalanine and to a lesser degree by dihydrophenylalanine. Molecular parameters of the previously isolated tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from E. coli (Schoner, R., and Herrmann, K.M. (1976) J. Biol. Chem. 251, ) are compared with those of the phenylalanine-sensitive isoenzyme from the same organism.PMID:
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External link. Please review our .Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors.
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2005 Oct 14;280(41):34530-7. Epub
2005 Aug 15.Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors.1, , , .1Departments of Pharmacology and Medicine, SUNY Upstate Medical University, Syracuse, New York , USA.AbstractInositol 1,4,5-trisphosphate (IP(3)) receptors form tetrameric, IP(3)-gated channels in endoplasmic reticulum membranes that govern the release of Ca(2+) from this organelle. In response to activation of certain G protein-coupled receptors that persistently elevate IP(3) concentration, IP(3) receptors are ubiquitinated and degraded by the ubiquitin-proteasome pathway. IP(3) receptor ubiquitination is mediated by the ubiquitin-conjugating enzyme, (mam)Ubc7, a component of the endoplasmic reticulum-associated degradation pathway. However, the mechanism by which ubiquitinated IP(3) receptors are transferred to the proteasome is not known. Here, we examine this process and show in several mammalian cell types that the ATPase p97 associates with IP(3) receptors in response to hormonal stimuli that induce IP(3) receptor ubiquitination. To examine the functional relevance of the p97 interaction with IP(3) receptors, we stably and specifically reduced p97 protein levels by 62 +/- 3% in Rat-1 fibroblasts using RNA interference. In these cells, endothelin-1-induced IP(3) receptor degradation was markedly retarded and the accumulation of ubiquitinated IP(3) receptors was markedly enhanced. These effects were reversed by expression of exogenous p97. In addition, Ufd1 and Npl4, which complex with p97, also associated with IP(3) receptors upon hormonal stimulation. We conclude that the p97-Ufd1-Npl4 complex couples ubiquitinated IP(3) receptors to proteasomal degradation and, thus, plays a key role in IP(3) receptor processing. These data also establish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalian cells.PMID:
[PubMed - indexed for MEDLINE] A, αT3-1 cells were stimulated with GnRH (0.1 μm) for the times indicated without (lanes 1–4) or with 1-h preincubation with 1 μm bortezomib (lane 5). Cells were then harvested and lysed, and IP3R1 was immunoprecipitated with anti-IP3R1. Samples were then electrophoresed and immunoblotted with anti-ubiquitin, anti-IP3R1, anti-p97, anti-Ufd1, anti-Npl4, and anti-Ufd2. B, Rat-1 cells were incubated for times indicated with 10 nm ET1 without (lanes 1–3) or with 1h preincubation with 1 μm bortezomib (lanes 4 – 8). Cells were then harvested and lysed, and IP3R1 was immunoprecipitated with anti-IP3R1. Samples were then electrophoresed and immunoblotted with anti-ubiquitin and anti-IP3R1. C, Rat-1 cells were incubated with 100 nm ET1 for the times indicated without or with 1h preincubation with 1 μm bortezomib. Cells were then harvested, lysates were prepared, and IP3R1 immunoreactivity was assessed, quantitated, and expressed as percentage of immunoreactivity at time 0. D and E, Rat-1 cells were incubated with 10 nm ET1 for the times indicated without or with 1 μm thapsigargin. Cells were then lysed, IP3R1 was immunoprecipitated with anti-IP3R1, and samples were immunoblotted as described for A. Proteins migrated as follows: polyubiquitinated IP3R1 at 275–380 kDa, IP3R1 at 260 kDa, p97 at 97 kDa, Ufd1 at 40 kDa, Npl4 at 60 kDa, and Ufd2 at 146 kDa.J Biol Chem. ;280(41):.A, sequence and predicted secondary structure of the short hairpin RNA that yields the siRNA that targets p97 mRNA. B, Rat-1 cells expressing three different control siRNA sequences (lanes 1–3) or p97 siRNA (lanes 4 – 6) were harvested and lysed, and equal amounts of cell protein were electrophoresed and immunoblotted with anti-p97, anti-HSP90, anti-Ufd2, anti-calnexin, anti-Ufd1, and anti-Sec61β. Proteins detected migrated as follows: p97 at 97 kDa, HSP90 at 90 kDa, Ufd2 at 146 kDa, calnexin at 90kDa, Ufd1 at 40 kDa, and Sec61β at 14 kDa. The histogram shows combined quantitated immunoreactivity from three independent experiments with * indicating significant differences (p & 0.05) from ran cell values by Welch’s unpaired t test. C, ran and p97 cells were stimulated with 100 nm ET1, and cytosolic free Ca2+ concentration was recorded. Data shown are mean ± S.E. of seven ind any differences between ran and p97 cells were not significant (p & 0.2 by unpaired t test).J Biol Chem. ;280(41):.A, ran and p97 cells were harvested, homogenized, and fractionated to prepare cytosol, membrane, and nuclear fractions, as well as total cell lysates. Equal amounts of protein from each fraction were then electrophoresed and immunoblotted with anti-ubiquitin. B, ran and p97 cells were incubated with 25 μg/ml cycloheximide for the times indicated, and equal amounts of cell lysates were electrophoresed and immunoblotted with anti-ubiquitin. C, ran and p97 cells were incubated without or with 20 μg/ml ALLN for 4 h, after which ALLN was removed, and cells were washed and allowed to recover for the times indicated. Equal amounts of cell protein were then electrophoresed and immunoblotted with anti-p53 and anti-p27.J Biol Chem. ;280(41):.A, ran and p97 cells were incubated with 10 nm ET1 for the times indicated. IP3R1 was then immunoprecipitated with anti-IP3R1 and was electrophoresed and immunoblotted with anti-ubiquitin and anti-IP3R1. B, quantitated ubiquitin immunoreactivity associated with IP3R1 expressed as a percentage of that associated with IP3R1 in ET1-stimulated ran cells at 20 * denotes p & 0.05, when comparing ran and p97 cells at each time point, by Welch’s unpaired t test. C and D, ran and p97 cells were stimulated with 10 nm ET1 for 60 min in the presence of 1 μm bortezomib. IP3R1 was then immunoprecipitated, processed, and quantitated as described for A and B. E and F, ran and p97 cells were incubated with 10 nm ET1 for the times indicated. Cells were then harvested and lysed, and equal amounts of cell protein were electrophoresed and immunoblotted with anti-IP3R1 and anti-IP3R3. Quantitated immunoreactivity of IP3R1 (squares) and IP3R3 (triangles) are expressed as percentage of immunoreactivity at time 0; * denotes p & 0.05, when comparing ran and p97 cells at each time point, by unpaired t test. G, p97 cells stably transfected with either empty vector or HA-p97 and ran cells were harvested and lysed, and equal amounts of cell protein were electrophoresed and immunoblotted with anti-HA (upper panel), anti-p97 (middle panel), or anti-Ufd2 (lower panel). H and I, p97 cells stably transfected with either empty vector (open circles) or HA-p97 (filled circles) and ran cells (open squares) were stimulated and analyzed as in B and F, * denotes significant differences (p & 0.05) from ran cell values.J Biol Chem. ;280(41):.Publication TypesMeSH TermsSubstancesGrant SupportFull Text SourcesOther Literature SourcesMiscellaneous
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