Determination of thiourea and its methyl derivatives by hypoiodite oxidation, and iodine monochloride end point; iodine bromide end point in the titration of thiourea with iodate

1957 ◽  
Vol 156 (4) ◽  
pp. 276-280 ◽  
Author(s):  
G. S. Deshmukh ◽  
M. G. Bapat
1986 ◽  
Vol 51 (10) ◽  
pp. 2077-2082 ◽  
Author(s):  
Jan Langmaier ◽  
František Opekar

Gold porous membrane electrode has been used for the potentiometric determination of small amounts of sulfur dioxide absorbed in the solutions of sodium tetrachloromercurate or sodium hydroxide. Sulfur dioxide is released by the reaction with an acid into a stream of nitrogen and led to the electrode immersed into the solution of iodine monochloride. Part of SO2 penetrates through the membrane pores into the solution where it is oxidized. The electrode redox potential change is a measure of the SO2 concentration in the absorption solution. In the solution of 1 . 10-5 M[ICl2]- in 0.02 M-HClO4 the limit of quantitation was found to be 0.07 ng SO2 . ml-1. The relative standard deviations of 1.4% and 2.5% were found for the determinations of 10 ng and 0.5 ng of SO2, respectively. Higher concentrations of H2S interfere only in the hydroxide solution. About 10 samples can be analyzed per one hour.


1980 ◽  
Vol 45 (8) ◽  
pp. 2364-2370 ◽  
Author(s):  
Antonín Holý ◽  
Erik De Clercq

Reaction of 3',5'-di-O-benzoyl-6-methyl-2'-deoxyuridine (IIa) with elementary bromine or iodine afforded 5-halogeno derivatives IIc and IId which on methanolysis gave 5-bromo-6-methyl-2'-deoxyurine (Ic) and 5-iodo-6-methyl-2'-deoxyurine (Id), respectively. The CD spectra of Ic, Id and 6-methyl-2'-deoxyuridine (Ia) are compared and discussed with regard to determination of the nucleoside conformation. Unlike 5-bromo- and 5-iodo-2'-deoxyuridine, the 6-methyl derivatives Ic and Id exhibit neither antibacterial nor antiviral activity. Nor do they exert any antimetabolic effect on the de novo DNA synthesis in primary rabbit kidney cells.


Author(s):  
Diana Spiegelberg ◽  
Jonas Stenberg ◽  
Pascale Richalet ◽  
Marc Vanhove

AbstractDesign of next-generation therapeutics comes with new challenges and emulates technology and methods to meet them. Characterizing the binding of either natural ligands or therapeutic proteins to cell-surface receptors, for which relevant recombinant versions may not exist, represents one of these challenges. Here we report the characterization of the interaction of five different antibody therapeutics (Trastuzumab, Rituximab, Panitumumab, Pertuzumab, and Cetuximab) with their cognate target receptors using LigandTracer. The method offers the advantage of being performed on live cells, alleviating the need for a recombinant source of the receptor. Furthermore, time-resolved measurements, in addition to allowing the determination of the affinity of the studied drug to its target, give access to the binding kinetics thereby providing a full characterization of the system. In this study, we also compared time-resolved LigandTracer data with end-point KD determination from flow cytometry experiments and hypothesize that discrepancies between these two approaches, when they exist, generally come from flow cytometry titration curves being acquired prior to full equilibration of the system. Our data, however, show that knowledge of the kinetics of the interaction allows to reconcile the data obtained by flow cytometry and LigandTracer and demonstrate the complementarity of these two methods.


1954 ◽  
Vol 100 (1) ◽  
pp. 81-88 ◽  
Author(s):  
Donald Greiff ◽  
Henry Pinkerton

A vacuum sublimation apparatus is described which will permit, (a) the removal of water from virus suspensions at temperatures ranging down to –80°C., (b) continuous operation with a minimum of attention from the investigator, (c) sealing off of samples at operating pressures (10–5 mm. Hg), (d) simultaneous lyophilization of aliquot samples at different temperatures, (e) isolation of a portion of the apparatus without disturbing the remainder of the system, and (f) determination of the end-point of sublimation without disturbing the samples. The time required for drying 0.1 ml. of influenza virus suspension was shown to increase markedly with decrease of temperature, 8 days being required for dehydration at –80°C. in contrast to 2 days at –30°C. and 1 day at 0°C.


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