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"Pembentukan kompleks Ni(II) dan 1,10-Phenanthroline (C12H8N2/Phen) dengan penambahan dithizone (C13H12N4S/HDz) pada antarmuka heksana-air telah dipelajari dengan metode spektrofotometri melalui pengukuran langsung dengan metode centrifugal liquid membrane(CLM). Ion Ni(II) dengan Phen membentuk kompleks kation Ni(C12H8N2) 22+atau NiPhen22+. Kompleks tersebut terlarutdalam fasa air serta memiliki dua panjang gelombang maksimum, λmaks yaitu 270 dan 292 nm. Pengamatan pembentukan kompleks dilakukan terhadap variasi pH dan konsentrasi ligan. Kondisi pH menyebabkan protonasi yang berpengaruh terhadap jumlah kompleks yang terbentuk. Pada variasi konsentrasi ligan, semakin besar konsentrasinya, jumlah kompleks yang terbentuk semakin banyak. Berdasarkan metode Batch, penambahan ligan HDz pada kompleks kation NiPhen 2 2+ menghasilkan kompleks asosiasi ion Ni(C13H11N4S)2(C12H8N2) atau NiDz 2Phen yang memilik iλ maks403 nm, dan terekstrak dalam fasa organik. Hasil Pengukuran menggunakan metode CLM, diketahui kompleks NiDz2 Phen terbentuk pada antarmuka heksana-air dengan λ maks 523 nm. Perbandingan konsentrasi ligan Phen dengan HDz mempengaruhi laju awal pembentukan kompleks NiDz2 Phen. Semakin besar konsentrasi ligan Phen, laju awal pembentukan kompleks sinergis semakin cepat. Data yang diperoleh menggunakan metode CLM menunjukkan bahwatetapan laju pembentukan kompleks sinergis NiDz2 Phen pada antarmuka, ksebesar 0,30 s-1.

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AbstractComplex formation of Ni(II) and 1,10-phenanthroline (C12H8N2/Phen) with the addition of dithizone (C13H12N4S/HDz)at the hexane-water interface has been studied by direct measurement spectrophotometry using the centrifugal liquid membrane (CLM) method. Ni(II) ion with Phen formed a cationic complex of Ni(C12H8N2) 22+or NiPhen22+. That complex dissolved in the aqueous phase and had two UV absorption spectrum maxima wavelengths, λ max 270 and 292nm. Observation of complex formation was performed variations of pH and ligand concentration. The pH caused protonation that affected the amount of the formed complex. With the variations of ligand concentrations, the greater was the concentration of ligands the greater was the formed complex. Based on the Batch method, the HDz ligand addition into the NiPhen 2 2+ cationic complex produced ionassociation complex of Ni(C13H11N4S)(C12H8N2) orNiDz2Phen atλmax 403 nm, and is extracted in the organic phase. Measurement results using CLM method showed that NiDz2 Phen complex was formed at hexane-water interface with λ max 523 nm. Comparison of Phen with HDz ligand concentrations affected the initial formation rate of NiDz2 Phen complex. The greater concentration of Phen ligand increased the initial rate of formation for synergistic complex. The obtained data using CLM method indicated that the synergistic complex formation rate constant of NiDz2 Phen at the interface, k was 0.30 s-1."

"Protein profiling with high-throughput proteomic technology, SELDI-TOF, is a new potential tool for diagnosis of human diseases. This advanced technique has increasingly been used for the detection of disease biomarker. However, analytical reproducibility is a significant challenge in SELDI-TOF profiling in order to have confidence in the results. Here, we showed a simple step to improve its analytical performance. IMAC 30-Cu Protein Chip was used to incubate denaturated samples to increase the number of peak detection and decrease peak intensity coefficient of variation. Incubation of denaturated samples overnight at 4oC increased significantly reproducibility and quality of proteomic profile of SELDI-TOF MS for IMAC30-Cu ProteinChip. This strategy could be applied to address reproducibility issue in protemictechnology in protein profiling."

"The book explain about proteomic technologies, such as protein biochips, protein-protein interactions, and proteome analysis in situ. The section on applications includes bioinformatics, Alzheimer's disease, neuroproteomics, plasma and T-cell proteomics, differential phosphoproteome analysis and biomarkers, as well as pharmacogenomics."

"This book includes, ABPP methodology (introduction and overview), activity-based protein profiling for natural product target discovery, photoaffinity labeling in activity-based protein profiling, and, functional analysis of protein targets by metabolomic approaches. "

"The book encompasses a wide range of topics, from muscle and meat proteomics to acute phase proteins and proteomics in aquaculture, to name but a few. The book summarily presents the state of the art in farm animal proteomics research in Europe, providing readers with interesting examples of the applications of this set of advanced technologies as well as useful contact details of colleagues with expertise in the field. Furthermore the book will provide an insight for proteomic specialists in demonstrating the breadth of applications that their technology can have in animal and food research."

"An update to the popular guide to proteomics technology applications in biomedical research Building on the strength of the original edition, this book presents the state of the art in the field of proteomics and offers students and scientists new tools and techniques to advance their own research. Written by leading experts in the field, it provides readers with an understanding of new and emerging directions for proteomics research and applications. Proteomics for Biological Discovery begins by discussing the emergence of proteomics technologies and summarizing the potential insights to be gained from proteome-level research. The tools of proteomics, from conventional to novel techniques, are thoroughly covered, from underlying concepts to limitations and future directions. Later chapters provide an overview of the current developments in post-translational modification studies, structural proteomics, biochemical proteomics, applied proteomics, and bioinformatics relevant to proteomics. Chapters cover: Quantitative Proteomics for Differential Protein Expression Profiling; Protein Microarrays; Protein Biomarker Discovery; Biomarker Discovery using Mass Spectrometry Imaging; Protein-Protein Interactions; Mass Spectrometry Of Intact Protein Complexes; Crosslinking Applications in Structural Proteomics; Functional Proteomics; High Resolution Interrogation of Biological Systems via Mass Cytometry; Characterization of Drug-Protein Interactions by Chemoproteomics; Phosphorylation; Large-Scale Phosphoproteomics; and Probing Glycoforms of Individual Proteins Using Antibody-Lectin Sandwich Arrays. Presents a comprehensive and coherent review of the major issues in proteomic technology development, bioinformatics, strategic approaches, and applications Chapters offer a rigorous overview with summary of limitations, emerging approaches, questions, and realistic future industry and basic science applications Features new coverage of mass spectrometry for high throughput proteomic measurements, and novel quantitation strategies such as spectral counting and stable isotope labeling Discusses higher level integrative aspects, including technical challenges and applications for drug discovery Offers new chapters on biomarker discovery, global phosphorylation analysis, proteomic profiling using antibodies, and single cell mass spectrometry Proteomics for Biological Discovery is an excellent advanced resource for graduate students, postdoctoral fellows, and scientists across all the major fields of biomedical science"

"Toxicogenomics is the integration of genomics to toxicology. This technology is a powerful tool for collecting information from a large number of biological samples simultaneously and thus it is very useful for large-scale screening of potential toxicants.Toxicogenomics : a powerful tool for toxicity assessment provides up-to-date state-of-the-art information presented by the recognized experts, and is therefore an authoritative source of current knowledge in this field of research. The potential link between toxicology, genetics and human diseases makes this book very useful to investigators in many and varied disciplines of science and toxicology. "