• Bulletin of the Korean Chemical Society
• /
• v.26 no.11
• /
• pp.1692-1694
• /
• 2005

Spent nuclear fuel is reprocessed commercially by the chemical process to recover U and Pu. Recently, new salt-free reagents to separate plutonium and neptunium from uranium suitable for use in a single cycle flowsheet have been developed. Acetohydroxamic acid $(CH_3CONHOH)$ has been taken much interest in as a complexing agent capable of selective stripping of tetravalent actinides from U(VI) when actinides are present in the solvent stream of the advanced PUREX process. Additionally acetohydroxamic acid will rapidly reduce Np(VI) to inextractable Np(V) thus allowing the separation of Np from U. In this study, the rate equation for the reduction of Np(VI) to Np(V) in nitric acid aqueous solution has been determined as: $-[NpO_2^{2+}]$/dt = $k[NpO_2^{2+}]$[AHA] with k = 191.2 ${\pm}$ 11.2 $M^{-1}s^{-1}$ at 25 ${\pm}$ 0.5 ${^{\circ}C}$ and $[HNO_3]$ = 1.0 M. Comparison with other reductants available in the literature, acetohydroxamic acid is a strong one for $NpO_2^{2+}$.

• Journal of Life Science
• /
• v.10 no.6
• /
• pp.558-563
• /
• 2000

Effect of inhibitors on Vibrio parahaemolyticus cell growth and its urease activity was studied. The growth of the bacterium and the enzyme activity were inhibited by the addition of 0.02% p-hydroxymercuric benzoate, $HgCl_2$and $AgNO_3$. However, same concentration of boric acid, thallium acetate and $Pb(NO_3)_2$ did not affect the cell growth but inhibited urease activity by 25%, 29%, and 38%, respectively. Acetohydroxamic acid was the most potent inhibitor on cell growth by inhibiting 40% but did not affect urease activity. To investigate the effect of inhibitors on urease activity, urease was purified and confirmed on SDS-PAGE. The purified urease was inhibited 100% by the addition of 1 mM acetohydroxamic acid and $AgNO_3$but no inhibition was occurred by the addition of the same concentration of thallium acetate. and the addition of 0.01 mM of $HgCl_2$ and acetohydroxamic acid inhibited the purified urease activity by 39% and 24%, respectively. On 0.1 millimolar basic, acetohydroxamic acid and $HgCl_2$inhibited 4 times more active in urease inhibition than p-hydroxymercuric benzoate whereas no inhibition was occurred either thallium acetate or $Pb(NO_3)_2$.

• Archives of Pharmacal Research
• /
• v.9 no.3
• /
• pp.163-167
• /
• 1986

Twenty six urea analogues, most of which have already been approved for human use, were tested for their antiurease activity in vitro. Cell-free extracts obtained from a clinical isolate of Proteus mirabilis was used as the source of enzyme. Acetohydroxamic acid which is a proven potent urease inhibitor but not approved for human use was again shown to be the most active compound among the tested. Phenacemide, cycloserine, and deferoxamine were demonstrated to be moderate inhibitors. Oxtetracycline, trimethoprim, and cefamandole revealed a demonstrable antiruease activity, but only at very high concentrations. The antiurease activity of cycloserine, trimethoprim, and cefamandole was pH dependent-only active at acidic pH. The inhibitory activity of acetohydroxamic acid however was independent of change in pH. The inhibitory activity of acetohydroxamic acid however was independent of change in pH. Hydrogen ion concentration plays an important role in urease activity and acidification (pH 5. 5) alone eliminates approximately 65% of the enzymic activity. Adjustment of pH therefore appears to be an important adjunct in reducing unrease activity and should always be studied to maximize the effcacy of antiurease compounds under investigation.

• Nuclear Engineering and Technology
• /
• v.54 no.9
• /
• pp.3580-3585
• /
• 2022

The thermal stability of carbohydrazide, hydrazine nitrate, acetohydroxamic acid in nitric acid solutions has been studied at atmospheric pressure and above atmospheric pressure. The volumes of gaseous products of thermolysis and the maximum rate of gas evolution have been determined at atmospheric pressure. It has been shown that, despite the high rate of gas evolution and large volumes of evolved gases, the conditions for the development of autocatalytic oxidation are not created. Exothermic processes are observed in a closed vessel in the temperature range of 50-250 ℃. With an increase in the concentration of nitric acid, the temperatures of the onset of exothermic effects for all mixtures decrease, and the values of the total thermal effects of reactions increase, to the greatest extent for solutions with carbohydrazide.

• Journal of the Korea Organic Resources Recycling Association
• /
• v.29 no.4
• /
• pp.5-13
• /
• 2021

Ammonia, primarily originating from urinary urea of the livestock manure, is known to play as a major precursor of fine particulate matter (PM2.5) generation which leads to a decrease in air quality and to harmful effects on public health. The objective of this study was to evaluate the effect of acetohydroxamic acid (AHA) addition on inhibition of ammonia conversion from urea. The experiment was performed at different urea concentration (500-4,000 mg Urea-N/L), AHA concentration (0-4,000 mg AHA/L), pHs (pH 6-10), and temperature (10-35℃). The result showed that the urease inhibition efficiency increased at higher concentration of AHA. However, the specific urease inhibition activity decreased at higher pH, showing 867.1±6.7 Unit/g AHA at pH 6 and 1,167.9±17.4 Unit/g AHA at pH 10, respectively. Decreased urease inhibition efficiency at both AHA and control was observed at higher temperature. This finding indicates that AHA can be used as the urease inhibitor for reducing ammonia emission in the management of livestock manure.

• Proceedings of the Korean Radioactive Waste Society Conference
• /
• 2006.06a
• /
• pp.203-203
• /
• 2006

• Proceedings of the Korean Radioactive Waste Society Conference
• /
• 2005.06a
• /
• pp.435-435
• /
• 2005

• Korean Journal of Pharmacognosy
• /
• v.33 no.1 s.128
• /
• pp.13-17
• /
• 2002

Helicobacter pylori infection is associated with type B gastritis, peptic ulcer, and gastric cancer. The vacuolation of cells induced by H. pylori is thought to be essential for the initiation and maintenance of gastric infection. The roles of H. pylori cytotoxin, urease, and ammonia in the vacuolation of HeLa cells were determined. Ammonium chloride augmented the neutral red uptake induced by H. pylori toxin. Acetohydroxamic acid (AHA) failed to block the neutral red uptake induced by H. pylori toxin. Leweifang significantly prevented the vacuolation of HeLa cells induced by H. pylori toxin or H. pylori toxin and ammonium chloride. Further investigation is required to determine the mechanisms of Leweifang for the inhibition of vacuole formation of eukaryotic cells in response to the H. pylori toxin.

• Microbiology and Biotechnology Letters
• /
• v.20 no.5
• /
• pp.519-526
• /
• 1992

The gene coding for urease of alkalophilic Bacillus pasteurii had been cloned in Escherichia coli previously. The urease protein was purified 63.1-fold by TEAE-cellulose, DEAE-Sephadex A-50, Sephadex G-150 and Sephadex G-200 chromatographies with a 7.3% yield from the sonicated fluid of the E. coli HB1Ol(pBUll) encoding B. pasteurii urease gene. The ureases of E. coli (pBUll) and B. pasteurii possessed as a $K_m$ for urea, 42.1 mM and 40.4 mM, respectively. They hydrolyzed urea with $V_{max}$ of 86.9$\mu$mol/min and 160$\mu$mol/min, respectively. Both ureases were composed with four subunits (Mrs 67,000) and a subunit (Mr 20,000). The molecular weight of both native enzymes was Mr 280,OOO$pm$10,000 determined by gel filtration chromatography and Coomassie blue staining of the subunits. The optimal reaction pH of both ureases were pH 7.5. The ureases were stabled in pH 5.5-10.5. The optimal reaction temperature of both ureases were $60^{\circ}C$, and the ureases were stable for an hour at $50^{\circ}C$, 40min at $60^{\circ}C$ and 10 min at $70^{\circ}C$ The activity of both enzymes were inhibited completely by $Ag^{2+}$, $Hg^{2+}$, $Zn^{2+}$, $Cu^{2+}$, and were inhibited 60% by CoH, 30% by $Fe^{2+}$ and 10% by $Pb^{2+}$. However it was increased by the addition of $Sn^{2+}$, $Mn^{2+}$, $Mg^{2+}$ at concentration of $1{\times}10^{-3}$M. Both ureases were inhibited completely by p-CMB and acetohydroxamic acid. The urease expressed in E. coli (pBU11) was inhibited 70% by SDS. The urease of B. pasteurii was inhibited 40% by hydroxyurea, whereas the recombinant urease of E. coli strain was inhibited 17%. Both enzymes were not inhibited by cyclohexanediaminetetraacetic acid (CDTA) and ethylendiaminetetraacetic acid (EDTA).

• Microbiology and Biotechnology Letters
• /
• v.45 no.3
• /
• pp.265-270
• /
• 2017

A key virulence factor for urinary tract pathogens is the enzyme urease, which catalyzes the hydrolysis of urea into ammonium ions and carbonic acid. Urease activity plays an important role in the pathogenesis of urinary tract infection. In this study, the inhibitory effect of zerumbone against six urease-producing bacteria (Klebsiella oxytoca, K. pneumoniae, Morganella morganii, Proteus mirabilis, P. vulgaris, and Staphylococcus saprophyticus) and their urease activities were evaluated. The results of the minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) tests showed that zerumbone had antibacterial effect against these six urease-producing bacteria. The MIC and MBC of zerumbone ranged from 0.5 to 2 mM and 1 to 4 mM, respectively. In the urease inhibitory assay, zerumbone showed better urease inhibition ($56.28{\pm}2.45-37.83{\pm}3.47%$) than the standard urease inhibitor, acetohydroxamic acid ($40.46{\pm}1.94-22.99{\pm}3.53%$). However, zerumbone did not affect the levels of the urease subunit. These results clearly indicated that zerumbone has antibacterial potential against urease-producing bacteria and possesses excellent bacterial urease inhibition properties.