Biuret
Biuret Reaction
Allophanate Hydrolase
Triazines
Colorimetry
Daily and alternate day supplementation of urea or biuret to ruminants consuming low-quality forage: I. Effects on cow performance and the efficiency of nitrogen use in wethers. (1/12)
Two experiments were conducted to determine the influence of supplemental nonprotein N (NPN) provided daily (D) or every other day (2D) on ruminant performance and N efficiency. Treatments included an unsupplemented control (CON) and a urea (28.7% CP) or biuret (28.6% CP) supplement provided D or 2D at 0700. In Exp. 1, five wethers (39 +/- 1 kg BW) were used in an incomplete 5 x 4 Latin square with four 24-d periods to determine the influence of supplemental NPN source and supplementation frequency (SF) on the efficiency of N use in lambs consuming low-quality grass straw (4% CP). The amount of CP supplied by each supplement was approximately 0.10% of BW/d (averaged over a 2-d period). In Exp. 2, 80 Angus x Hereford cows (540 +/- 8 kg BW) in the last third of gestation were used to determine the effect of NPN source and SF on cow performance. The NPN treatments were formulated to provide 90% of the estimated degradable intake protein requirement. The supplemented treatments received the same amount of supplemental N over a 2-d period; therefore, the 2D treatments received double the quantity of supplemental N on their respective supplementation day than the D treatments. In Exp. 1, total DM, OM, and N intake; DM, OM, and N digestibility; N balance; and digested N retained were greater (P < 0.03) for supplemented than for CON wethers, with no difference (P > 0.05) between NPN sources or SF. Plasma urea-N (PUN) was increased with N supplementation compared with CON (P < 0.01), and urea treatments had greater PUN than biuret (P < 0.01). In addition, PUN was greater (P = 0.02) for D than for 2D treatments. In Exp. 2, pre- and postcalving (within 14 d and 24 h after calving, respectively) cow weight and body condition score change were more positive (P < 0.05) for supplemented groups than for CON. These results suggest that supplements containing urea or biuret as the primary source of supplemental N can be effectively used by lambs and cows consuming low-quality forage, even when provided every other day. (+info)Daily and alternate-day supplementation of urea or biuret to ruminants consuming low-quality forage: II. Effects on site of digestion and microbial efficiency in steers. (2/12)
Five steers (491 +/- 21 kg BW) were used in an incomplete 5 x 4 Latin square with four 24-d periods to determine the influence of supplemental non-protein N (NPN) source and supplementation frequency (SF) on nutrient intake and site of digestion in steers consuming low-quality grass straw (4% CP). Treatments (TRT) included an unsupplemented control and a urea- or biuret-containing supplement placed directly into the rumen daily (D) or every other day (2D) at 0700. The NPN treatments were formulated to provide 90% of the estimated degradable intake protein requirement. Daily TRT were supplemented CP at 0.04% of BW/d, whereas the 2D TRT were supplemented at 0.08% of BW every other day. Therefore, all supplemented TRT received the same quantity of supplemental CP over a 2-d period. Forage OM intake was not affected (P > 0.05) by NPN supplementation, NPN source, or SF; however, total OM and N intake were increased (P < 0.01) with CP supplementation. Duodenal flow of N was greater (P = 0.04) with CP supplementation compared with the control. In addition, duodenal bacterial N flow was increased with CP supplementation (P = 0.04) and for biuret compared with urea (P < 0.01). Bacterial efficiency (g bacterial N/kg OM truly digested in the rumen) was greater (P = 0.05) for biuret than for urea. Apparent total-tract N digestibility was increased with NPN supplementation (P < 0.01) but not affected by NPN source or SF. These results suggest that urea or biuret can be used effectively as a supplemental N source by steers consuming low-quality forage. (+info)Daily and alternate-day supplementation of urea or biuret to ruminants consuming low-quality forage: III. Effects on ruminal fermentation characteristics in steers. (3/12)
Five ruminally and duodenally cannulated steers (491 +/- 21 kg BW) were used in an incomplete 5 x 4 Latin square with four 24-d periods to determine the influence of supplemental nonprotein N (NPN) source and supplementation frequency (SF) on the dynamics of ruminal fermentation in steers consuming low-quality grass straw (4% CP). Treatments (TRT) included an unsupplemented control (CON) and a urea or biuret supplement that were placed directly into the rumen at 0700 daily (D) or every other day (2D). The NPN treatments were formulated to provide 90% of the estimated degradable intake protein requirement; therefore, the urea and biuret treatments received the same amount of supplemental N over a 2-d period. Daily TRT were supplemented with CP at 0.04% of BW/d, whereas the 2D TRT were supplemented at 0.08% of BW every other day. Forage was provided at 120% of the previous 5-d average intake in two equal portions at 0715 and 1900. Ruminal fluid was collected 0, 3, 6, 9, 12, and 24 h after supplementation on a day of and a day before supplementation for all TRT. Ruminal NH3-N increased (P < 0.04) with CP supplementation on the day all supplements were provided and on the day on which only daily supplements were provided compared with the CON. However, an NPN source x SF interaction (P = 0.03) on the day all supplements were provided indicated that NH3-N increased at a greater rate for urea as SF decreased compared with biuret. Ruminal NH3-N on the day only daily supplements were provided was greater (P = 0.02) for D compared with 2D. On the day all supplements were provided, D increased (P = 0.05) ruminal indigestible acid detergent fiber passage rate and ruminal fluid volume compared with 2D. These results suggest that urea or biuret can be used effectively as a supplemental N source by steers consuming low-quality forage without adversely affecting ruminal fermentation, even when provided every other day. (+info)Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. (4/12)
TrzF, the allophanate hydrolase from Enterobacter cloacae strain 99, was cloned, overexpressed in the presence of a chaperone protein, and purified to homogeneity. Native TrzF had a subunit molecular weight of 65,401 and a subunit stoichiometry of alpha(2) and did not contain significant levels of metals. TrzF showed time-dependent inhibition by phenyl phosphorodiamidate and is a member of the amidase signature protein family. TrzF was highly active in the hydrolysis of allophanate but was not active with urea, despite having been previously considered a urea amidolyase. TrzF showed lower activity with malonamate, malonamide, and biuret. The allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, was also shown to hydrolyze biuret slowly. Since biuret and allophanate are consecutive metabolites in cyanuric acid metabolism, the low level of biuret hydrolase activity can have physiological significance. A recombinant Escherichia coli strain containing atzD, encoding cyanuric acid hydrolase that produces biuret, and atzF grew slowly on cyanuric acid as a source of nitrogen. The amount of growth produced was consistent with the liberation of 3 mol of ammonia from cyanuric acid. In vitro, TrzF was shown to hydrolyze biuret to liberate 3 mol of ammonia. The biuret hydrolyzing activity of TrzF might also be physiologically relevant in native strains. E. cloacae strain 99 grows on cyanuric acid with a significant accumulation of biuret. (+info)Electroosmotic sampling. Application to determination of ectopeptidase activity in organotypic hippocampal slice cultures. (5/12)
(+info)Defining sequence space and reaction products within the cyanuric acid hydrolase (AtzD)/barbiturase protein family. (6/12)
(+info)Effects of dextran on five biuret-based procedures for total protein in serum. (7/12)
We evaluated the effect of dextran on values for total protein in serum as measured by the biuret method with five widely used automated instruments: the American Monitor Parallel; the Du Pont aca II; the Roche Cobas-Bio; the Kodak Ektachem 400; and the Beckman Astra 8. Dextran concentrations as great as 25 or 30 g/L had relatively little or no influence on total protein measurements by the latter three instruments. Dextran concentrations exceeding 6 g/L caused falsely low results with the aca, whereas the Parallel gave falsely high results when the dextran concentration exceeded 2 g/L. The aca total protein procedure could be protected from the interference by dextran concentrations up to 30 g/L by injecting 0.4-0.8 mL of ethylene glycol directly into the reagent pack before sampling. However, we could not eliminate the interference with the Parallel procedure by any simple means; we thus recommend that it not be used for measuring total protein in serum samples from patients who are being treated with dextran. (+info)Application of a silver-binding assay to the determination of protein in cerebrospinal fluid. (8/12)
We evaluated a silver-binding assay for use in measuring total protein in cerebrospinal fluid. The advantage of this procedure over other methods is that, because of its sensitivity, it requires only a 0.5-microL sample. The procedure, which takes approximately 40 min to complete, involves dilution of 0.5-microL samples to 1 mL with distilled water containing sodium dodecyl sulfate, followed by addition of glutaraldehyde and an ammoniacal silver solution. After color development for 30 min, the reaction is terminated with sodium thiosulfate and the absorbance is measured at 420 nm. This assay displayed within-run and day-to-day precision (CV) of 3.1% to 13% over the range of 210 to 1370 mg/L. It showed substantially less protein-to-protein variation than the Coomassie Blue dye-binding procedure when tested with albumin, globulin, and transferrin. It also yielded an accurate estimation of hemoglobin. Moreover, preliminary studies suggested that it was capable of quantifying immunoglobulin light chains and glycoproteins. In a study of 54 human cerebrospinal fluid samples, results of the silver-binding assay corresponded more closely with those obtained with a rate biuret assay (intraclass correlation coefficient = 0.91) than did either the dye-binding or classical Lowry methods. (+info)The biuret test is a medical/biochemical test used to detect the presence of peptide bonds, which are found in proteins. The test involves mixing a sample with a solution containing copper(II) sulfate and an alkaline substance, such as sodium hydroxide. If proteins are present in the sample, the copper ions will form a complex with the peptide bonds, resulting in a purple or violet color in the solution. The intensity of the color can be used to estimate the amount of protein present in the sample.
Biuret is actually a compound that is not related to proteins, but it was named after the same chemist as the biuret test. Biuret is a chemical compound with the formula CONHCONH2. It is formed by the reaction of two molecules of urea (CO(NH2)2) under heat. The biuret test does not detect biuret itself, but rather the peptide bonds found in proteins.
The Biuret reaction is a medical/biochemical test used to detect the presence of peptide bonds, which are found in proteins. The reagent used for this test contains copper(II) sulfate in an alkaline solution, and it works by forming a violet complex when it binds to two or more peptide bonds in a protein molecule.
When the Biuret reagent is added to a protein solution, the copper ions in the reagent bind to the nitrogen atoms of the peptide bonds, causing a color change from blue to violet. The intensity of the color correlates with the amount of protein present in the sample. This reaction can be used as a quantitative method for measuring protein concentration in a solution.
It is important to note that the Biuret reaction is not specific to proteins and can also occur with other compounds containing peptide bonds, such as some peptides and small molecules. Therefore, additional tests are often needed to confirm the presence of proteins in a sample.
Allophanate hydrolase is an enzyme that catalyzes the hydrolysis of allophanates, which are cyclic urea derivatives, to form carboxylic acids and ammonia. This enzyme plays a role in the metabolism of urea-containing compounds in some organisms. The systematic name for this enzyme is allophanate hydrolase (decyclizing).
Triazines are not a medical term, but a class of chemical compounds. They have a six-membered ring containing three nitrogen atoms and three carbon atoms. Some triazine derivatives are used in medicine as herbicides, antimicrobials, and antitumor agents.
Colorimetry is the scientific measurement and quantification of color, typically using a colorimeter or spectrophotometer. In the medical field, colorimetry may be used in various applications such as:
1. Diagnosis and monitoring of skin conditions: Colorimeters can measure changes in skin color to help diagnose or monitor conditions like jaundice, cyanosis, or vitiligo. They can also assess the effectiveness of treatments for these conditions.
2. Vision assessment: Colorimetry is used in vision testing to determine the presence and severity of visual impairments such as color blindness or deficiencies. Special tests called anomaloscopes or color vision charts are used to measure an individual's ability to distinguish between different colors.
3. Environmental monitoring: In healthcare settings, colorimetry can be employed to monitor the cleanliness and sterility of surfaces or equipment by measuring the amount of contamination present. This is often done using ATP (adenosine triphosphate) bioluminescence assays, which emit light when they come into contact with microorganisms.
4. Medical research: Colorimetry has applications in medical research, such as studying the optical properties of tissues or developing new diagnostic tools and techniques based on color measurements.
In summary, colorimetry is a valuable tool in various medical fields for diagnosis, monitoring, and research purposes. It allows healthcare professionals to make more informed decisions about patient care and treatment plans.
'Enterobacter cloacae' is a species of Gram-negative, facultatively anaerobic, rod-shaped bacteria that are commonly found in the environment, including in soil, water, and the gastrointestinal tracts of humans and animals. They are part of the family Enterobacteriaceae and can cause various types of infections in humans, particularly in individuals with weakened immune systems or underlying medical conditions.
E. cloacae is known to be an opportunistic pathogen, which means that it typically does not cause disease in healthy people but can take advantage of a weakened host to cause infection. It can cause a range of infections, including urinary tract infections, pneumonia, bacteremia (bloodstream infections), and wound infections.
E. cloacae is often resistant to multiple antibiotics, which can make treatment challenging. In recent years, there has been an increase in the number of E. cloacae isolates that are resistant to carbapenems, a class of antibiotics that are typically reserved for treating serious infections caused by multidrug-resistant bacteria. This has led to concerns about the potential for untreatable infections caused by this organism.