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Urea

About: Urea is a research topic. Over the lifetime, 21394 publications have been published within this topic receiving 382444 citations. The topic is also known as: carbamide & carbonic acid diamide.


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Journal ArticleDOI
TL;DR: Automated and manual direct methods for the determination of urea in blood or serum determine urea by the colored product formed when urea, in relatively weak acid solution, reacts with diacetyl monoxime in the presence of thiosemicarbazide and ferric ion.
Abstract: Automated and manual direct methods for the determination of urea in blood or serum are described. These methods determine urea by the colored product formed when urea, in relatively weak acid solution, reacts with diacetyl monoxime in the presence of thiosemicarbazide and ferric ion. Results are compared with those obtained by urease conversion of urea to ammonia and measurement of the ammonia by nesslerization.

1,074 citations

Journal ArticleDOI
TL;DR: A single gel is able to resolve an entire range from large proteins to small peptides, obviating the need for urea or other additives as used in other systems.

926 citations

Journal ArticleDOI
Jie Cai1, Lina Zhang1
TL;DR: The results from DSC and (13)C NMR indicated that LiOH/urea and NaOH/UREa aqueous solutions as non-derivatizing solvents broke the intra- and inter-molecular hydrogen bonding of cellulose and prevented the approach toward each other of the cellulose molecules, leading to the good dispersion of cellulOSE to form an actual solution.
Abstract: Rapid dissolution of cellulose in LiOH/urea and NaOH/urea aqueous solutions was studied systematically. The dissolution behavior and solubility of cellulose were evaluated by using (13)C NMR, optical microscopy, wide-angle X-ray diffraction (WAXD), FT-IR spectroscopy, DSC, and viscometry. The experiment results revealed that cellulose having viscosity-average molecular weight ((overline) M eta) of 11.4 x 104 and 37.2 x 104 could be dissolved, respectively, in 7% NaOH/12% urea and 4.2% LiOH/12% urea aqueous solutions pre-cooled to -10 degrees C within 2 min, whereas all of them could not be dissolved in KOH/urea aqueous solution. The dissolution power of the solvent systems was in the order of LiOH/urea > NaOH/urea >> KOH/urea aqueous solution. The results from DSC and (13)C NMR indicated that LiOH/urea and NaOH/urea aqueous solutions as non-derivatizing solvents broke the intra- and inter-molecular hydrogen bonding of cellulose and prevented the approach toward each other of the cellulose molecules, leading to the good dispersion of cellulose to form an actual solution.

808 citations

Journal ArticleDOI
TL;DR: These simulations suggest that urea denatures proteins via both direct and indirect mechanisms, and that through urea's weakening of water structure, water became free to compete with intraprotein interactions.
Abstract: Molecular dynamics simulations of the protein chymotrypsin inhibitor 2 in 8 M urea at 60 degrees C were undertaken to investigate the molecular basis of chemical denaturation. The protein unfolded rapidly under these conditions, but it retained its native structure in a control simulation in water at the same temperature. The overall process of unfolding in urea was similar to that observed in thermal denaturation simulations above the protein's T(m) of 75 degrees C. The first step in unfolding was expansion of the hydrophobic core. Then, the core was solvated by water and later by urea. The denatured structures in both urea and at high temperature contained residual native helical structure, whereas the beta-structure was completely disrupted. The average residence time for urea around hydrophilic groups was six times greater than around hydrophobic residues and in all cases greater than the corresponding water residence times. Water self-diffusion was reduced 40% in 8 M urea. Urea altered water structure and dynamics, thereby diminishing the hydrophobic effect and encouraging solvation of hydrophobic groups. In addition, through urea's weakening of water structure, water became free to compete with intraprotein interactions. Urea also interacted directly with polar residues and the peptide backbone, thereby stabilizing nonnative conformations. These simulations suggest that urea denatures proteins via both direct and indirect mechanisms.

803 citations

Journal ArticleDOI
TL;DR: In this article, a simple and precise method of assaying urease activity in soils is described, which involves determination of the ammonium released by urea-fixing activity when soil is incubated with tris(hydroxymethyl)aminomethane (THAM) buffer, urea solution, and toluene at 37°C for 2 h, ammonium release being determined by a rapid procedure involving treatment of the incubated soil sample with 2.5 M KC1 containing a urea inhibitor (Ag 2 SO 4 ) and steam distillation of
Abstract: A simple and precise method of assaying urease activity in soils is described. It involves determination of the ammonium released by urease activity when soil is incubated with tris(hydroxymethyl)aminomethane (THAM) buffer, urea solution, and toluene at 37°C for 2 h, ammonium release being determined by a rapid procedure involving treatment of the incubated soil sample with 2.5 M KC1 containing a urease inhibitor (Ag 2 SO 4 ) and steam distillation of an aliquot of the resulting soil suspension with MgO for 3.3 min. Studies reported showed that the optimal buffer pH and substrate (urea) concentration for assay of soil urease activity using THAM buffer are 9.0 and 0.02 M, respectively, and that the method described is satisfactory for assay of urease activity in ammonium-fixing soils.

776 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20231,000
20221,982
2021433
2020502
2019589
2018557