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Effects of urea,metal ions and surfactants on the binding of baicalein with bovine serum albumin

Journal of Pharmaceutical Analysis 2016年第4期6卷 256-267页

作者： Atanu Singha Roy amit kumar dinda Nitin kumar Pandey Swagata Dasgupta Department of Chemistry Indian Institute of Technology

The interaction of baicalein with bovine serum albumin（BSA） was investigated with the help of spectroscopic and molecular docking *** binding affinity of baicalein towards BSA was estimated to be in order of 10~5 M^（-1） from fluorescence quenching *** ΔH°（-5.66 ＋ 0.14 kJ/mol） and positive（ΔS°）（＋ 79.96 ＋ 0.65J/mol K） indicate the presence of electrostatic interactions along with the hydrophobic forces that result in a positive ΔS°.The hydrophobic association of baicalein with BSA diminishes in the presence of sodium dodecyl sulfate（SDS） due to probable hydrophobic association of baicalein with SDS,resulting in a negative ΔS°（-40.65 ＋ 0.87 J/mol K）.Matrix-assisted laser desorption ionization/time of flight（MALDI-TOF） experiments indicate a 1：1 complexation between baicalein and *** unfolding and refolding phenomena of BSA were investigated in the absence and presence of baicalein using steady-state and fluorescence lifetime *** was observed that the presence of urea ruptured the non-covalent interaction between baicalein and *** presence of metal ions（Ag~＋,Mg^（2＋）,Ni^（2＋）,Mn^（2＋）,Co^（2＋） and Zn^（2＋）） increased the binding affinity of ligand towards *** changes in conformational aspects of BSA after ligand binding were also investigated using circular dichroism（CD） and Fourier transform infrared（FT-IR） spectroscopic *** selectivity studies following molecular docking analyses indicated the binding of baicalein to site 1（subdomain MA） of BSA.

关键词： Bovine serum albumin(BSA) Baicalein Binding constant Fluorescence spectroscopy Molecular docking

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Immunofluorescence on paraffin embedded renal biopsies:Experience of a tertiary care center with review of literature

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World Journal of Nephrology 2016年第5期5卷 461-470页

作者： Geetika Singh Lavleen Singh Ranajoy Ghosh Devajit Nath amit kumar dinda Department of Pathology All India Institute of Medical SciencesNew Delhi 110029India

AIMTo describe the technique of immunofluorescence on paraffin embedded tissue sections and discuss the po-tential pitfalls with an in depth review of *** is integral to diagnostic renal pa-thology. Immunofluorescence on paraffin embedded renal biopsies （IF-P） after enzyme treatment has been described in literature, however has not found widespread use in renal pathology laboratories. In our laboratory proteinase K digestion of paraffn embedded renal biopsy material was standardized and applied prospectively in cases where immunofuorescence on fresh frozen tissue was non contributory or not possible. Diagnostic utility was assessed and in a cohort of cases comparison of intensity of staining with routine immunofuorescence was *** the 5-year study period, of the 3141 renal biopsies received IF-P was performed on 246 cases （7.7%） and was interpretable with optimal digestion in 214 cases （6.8%）. It was of diagnostic utility in the majority of cases, which predominantly included glomerular disease. Non-diagnostic IF-P was found in membranous nephropathy （2 of 11 cases）, membranoproliferative glomerulonephritis （2 of 32 cases）, lupus nephritis （1 of 25 cases）, post infectious glomerulonephritis （1 of 11 cases） and chronic glomerulonephritis （3 of 8 cases）. Comparing cases with both routine IF and IF-P, 35 of 37 showed either equal intensity or a minor difference in intensity of staining（1＋） for the diagnostic immunoglobulin/complement. Technically assessment of immunofluorescence on the paraffin embedded tissue was found to be easier with clearly observed morphology, however a false positive staining pattern was observed in under-digested tissue. CONCLUSIONAs a “salvage” technique, immunofuorescence on paraffn embedded renal biopsies is of great diagnostic utility, however not without pitfalls.

关键词： Immunofluorescence on paraffin section Renal biopsy Salvage technique Enzymatic digestion Proteinase KSnea

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