Biosorptive removal of Pb2+, Cd2+ and Zn2+ ions from water by agenaria vulgaris shell

Lagenaria vulgaris (LV) shell was used as a biosorbent for the removal of heavy metal ions, Pb2+, Cd2+ and Zn2+, from aqueous solutions. Experiments were carried out under batch conditions. The effects of contact time, initial pH, temperature and stirring speed on removal efficiency are presented. Sorption of the investigated metals was fast, reaching equilibrium after about 5 to 10 min, depending on the metal. Biosorption was highly pH-dependent, and the optimal pH for investigated metals was in the range of 4.5 to 6.0. The effects of temperature demonstrated that biosorption of the metals is a chemical process. SEM analysis revealed interesting morphological changes after acid refinement of the raw biosorbent and metal uptake that is related to the chemical nature of the biosorption process. EDX analysis of Lagenaria vulgaris biosorbent(LVB) before and after metal sorption revealed that the ion exchange mechanism was the principal sorption process. Fourier transform infrared spectroscopy (FTIR) analysis has shown that major functional groups (carboxyl and hydroxyl) on the biosorbent surface took part in the metal ion uptake process as active sites. The results obtained showed that Lagenaria vulgaris based biosorbent could be used as an effective and low-cost pre-treatment step for removal of toxic metals from wastewaters

Analytical techniques for multiplex analysis of protein biomarkers

Introduction: The importance of biomarkers for pharmaceutical drug development and clinical diagnostics is more significant than ever in the current shift toward personalized medicine. Biomarkers have taken a central position either as companion markers to support drug development and patient selection, or as indicators aiming to detect the earliest perturbations indicative of disease, minimizing therapeutic intervention or even enabling disease reversal. Protein biomarkers are of particular interest given their central role in biochemical pathways. Hence, capabilities to analyze multiple protein biomarkers in one assay are highly interesting for biomedical research. Areas covered: We here review multiple methods that are suitable for robust, high throughput, standardized, and affordable analysis of protein biomarkers in a multiplex format. We describe innovative developments in immunoassays, the vanguard of methods in clinical laboratories, and mass spectrometry, increasingly implemented for protein biomarker analysis. Moreover, emerging techniques are discussed with potentially improved protein capture, separation, and detection that will further boost multiplex analyses. Expert commentary: The development of clinically applied multiplex protein biomarker assays is essential as multi-protein signatures provide more comprehensive information about biological systems than single biomarkers, leading to improved insights in mechanisms of disease, diagnostics, and the effect of personalized medicine.</div

The nuclear cap-binding complex interacts with the U4/U6·U5 tri-snRNP and promotes spliceosome assembly in mammalian cells

The nuclear cap-binding complex (CBC) binds to the 7-methyl guanosine cap present on every RNA polymerase II transcript. CBC has been implicated in many aspects of RNA biogenesis; in addition to roles in miRNA biogenesis, nonsense-mediated decay, 3'-end formation, and snRNA export from the nucleus, CBC promotes pre-mRNA splicing. An unresolved question is how CBC participates in splicing. To investigate CBC's role in splicing, we used mass spectrometry to identify proteins that copurify with mammalian CBC. Numerous components of spliceosomal snRNPs were specifically detected. Among these, three U4/U6·U5 snRNP proteins (hBrr2, hPrp4, and hPrp31) copurified with CBC in an RNA-independent fashion, suggesting that a significant fraction of CBC forms a complex with the U4/U6·U5 snRNP and that the activity of CBC might be associated with snRNP recruitment to pre-mRNA. To test this possibility, CBC was depleted from HeLa cells by RNAi. Chromatin immunoprecipitation and live-cell imaging assays revealed decreased cotranscriptional accumulation of U4/U6·U5 snRNPs on active transcription units, consistent with a requirement for CBC in cotranscriptional spliceosome assembly. Surprisingly, recruitment of U1 and U2 snRNPs was also affected, indicating that RNA-mediated interactions between CBC and snRNPs contribute to splicing. On the other hand, CBC depletion did not impair snRNP biogenesis, ruling out the possibility that decreased snRNP recruitment was due to changes in nuclear snRNP concentration. Taken together, the data support a model whereby CBC promotes pre-mRNA splicing through a network of interactions with and among spliceosomal snRNPs during cotranscriptional spliceosome assembly