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MySQL Error: 1194 (Table 'pwn_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select * from pwn_comment where pid='587230' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\includes\db.inc.php:54] #1 dbbase_sql->query(select * from {P}_comment where pid='587230' and iffb='1' order by id limit 0,10) called at [D:\wwwroot\hs21cn2043\wwwroot\comment\module\CommentContent.php:167] #2 CommentContent() called at [D:\wwwroot\hs21cn2043\wwwroot\includes\common.inc.php:551] #3 printpage() called at [D:\wwwroot\hs21cn2043\wwwroot\comment\html\index.php:13]
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网友点评-By fluorescence 2D-DIGE and multidimensional LC-MS/MS evaluation. For the LC-MS-线缆测高仪,超声波测高仪, 手持式测高仪-上海交通大学科技园上海野豹企业发展公司
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发布于:2018-10-12 01:41:02  访问:56 次 回复: 篇
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By fluorescence 2D-DIGE and multidimensional LC-MS/MS evaluation. For the LC-MS
The strategy is termed steady isotope labeled proteome (SILAP). The SILAP process is determined by the absolute SILAC method [105], in which cultured cells are grown in steady isotope-labelled serum-free media with stable isotope labelled lysine and leucine. To demonstrate the technical capability of SILAP, columnar epithelial endocervical-1 (End1) and vaginal mucosal-2 (Vk2) cells had been grown in SILAC situations to create a SILAP library containing the secreted proteins. It was assumed that End1 and Vk2 cells are "normal" transformed cells of human origin and possess a secretory phenotype, and therefore, their secreted proteins would model the proteins present in human CVF. The secreted proteome from the cells were then determined by multidimensional LC-MS/MS analysis, right after MARS Hu6 abundant proteins depletion and SCX fractionation. In three independent experiments (replicates), 1211 proteins have been identified from the secreted proteome. With the total 1211 proteins identified, 236 have been detected in all 3 replicates. Fifteen potential protein Phorbol chemical information biomarkers for sPTB were chosen from the 236 proteins depending on the preceding reports in sPTB or other pregnancy-related situations. Steady isotope dilution LC-SRM assays were then designed to conduct relative quantification of those candidate PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/21231855 biomarkers in term and sPTB human CVF samples spiked with the SILAP internal regular. Elevated expression of desmoplakin isoform 1, stratifin, and thrombospondin 1 precursor in sPTB relative towards the handle group was statistically significant. In specific, desmoplakin isoform 1 peptide was quantified to be 70.7-fold larger within the sPTB samples as when compared with the handle samples. Moreover, stratifin peptide (42.4-fold) and thrombospondin 1 precursor peptide (five.1-fold) Oleandrin levels were significantly greater within the preterm birth patient samples. While the data indicated these three proteins could serve as possible protein biomarkers, the study was depending on a somewhat tiny cohort; additional validation is essential.Int. J. Mol. Sci. 2015, 16 six. Comments six.1. The Current Status of Proteomics for Pre-Eclampsia and Preterm BirthThe technolog.By fluorescence 2D-DIGE and multidimensional LC-MS/MS evaluation. For the LC-MS/MS analysis, individually pooled samples were ready from five maternal CVF samples, each and every of handle, PTL and sPTB. Non-protein interferences had been removed by acetone precipitation. The tryptic peptides had been separated into 80 fractions PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/28408716 by SCX chromatography and every single fraction was then analyzed on a Q-TOF-2 mass spectrometer coupled to a CapLC. Spectral counting was applied to assess the relative abundance of a protein. Twenty-eight in the identified proteins exhibited considerable differences in pairwise and progressive comparisons. Calgranulins A and B, annexins A3, S100 calcium-binding protein A7, and epidermal fatty acid binding protein were abundant in CVF and differentially present in PTL and sPTB samples, as have been the serum proteins -1-antitrypsin, 1-acid glycoprotein, haptoglobin precursor, serotransferrin precursor (transferrin), and vitamin D binding protein precursor [55]. Quantification of protein biomarker candidates by targeted proteomics is hampered by the troubles associated with all the preparation of labelled peptide references. One study took an opportunistic method to generate an entire labelled proteome, which was then made use of as internal standards to facilitate correct quantification of peptides, and proteins thereof, inside a biological sample [104].
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