Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A device, the enzyme thermistor, is described which is capable of measuring changes in heat due to enzymic reactions. The sensor, a thermistor, is in direct contact with the site of reaction through its placement in a microcolumn filled with an immobilised enzyme preparation. The substrate solution flows past the thermistor tip, and as much as approx. one half of the total heat evolved can be registered as temperature change, deltat. Glass-bound glucose oxidase (EC 1.1.3.4), penicillinase (EC 3.5.2.6), trypsin (EC 3.4.21.4) and urease (EC 3.5.1.5) were used for the determination of glucose, penicillin G, benzoyl-L-arginine ethyl ester and urea respectively. Linear relationships between the deltat recorded and the concentration of substrate were obtained in all cases.
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PMID:Determination of heat changes in the proximity of immobilised enzymes with an enzyme thermistor and its use for the assay of metabolites. 117 49

The hydrophobic nature of proteins is characterized by a degree of 2-p-toluidinonaphthalene-6-sulphonate (TNS) affinity to them and is pronounced quantitatively in the semi-saturated (C1/2) concentrations. This index correlates directly with the position of TNS emission maximum after the binding with proteins and reversely with the yield of fluorescence. The preparations of phosphofructokinase, lactate dehydrogenase, xantinoxidase, glyceratekinase, lysozyme, RNase during the long (1-2 h) contact with TNS change the values C1/2, that evidences for interaction with the hydrophobic indicator of new structures of protein molecule or for a change in the nature of its linkage itself. An attempt is made to characterize the accessible for TNS hydrophobic nature of individual proteins by a coefficient of molar hydrophobic nature which unites three mentioned characteristics. Serum albumin, insulin, glucogon, alpha chemotrypsin, DNase are most hydrophobic, pyruvate kinase, aldolase, urease, RNase--least hydrophobic, Glycerate kinase, pyruvate decarboxylase, phosphofructokinase, lactate dehydrogenase, alcohol dehydrogenase, xanthinoxidase, trypsin, lysozyme are in intermediate position.
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PMID:[Comparative characteristics of hydrophobic nature of certain proteins by their interaction with 2-p-toluidinonaphthalene-6-sulfonates]. 120 4

An experiment was conducted with ileally cannulated pigs to determine the apparent digestibility of amino acids and N in raw or heated conventional or low-trypsin-inhibitor soybeans. Six littermate barrows initially averaging 24 kg were fed cornstarch-based diets (10.5% CP, .68% lysine, 3,558 kcal of ME/kg) supplemented with raw (unheated), conventional soybeans; raw, low-trypsin-inhibitor soybeans; heated, conventional soybeans; heated, low-trypsin-inhibitor soybeans; or solvent-extracted soybean meal. Heating was achieved by autoclaving soybeans (after grinding) for 20 min at 110 degrees C. The urease activities of the two raw soybean sources were similar, but the trypsin inhibitor activity of the raw, low-trypsin-inhibitor soybeans was about one-half that of the raw, conventional soybeans. The lower trypsin inhibitor activity of the raw, low-trypsin-inhibitor soybeans was associated with an improvement in the apparent digestibility of amino acids and N compared with the raw, conventional soybeans (P less than .05). Heating reduced the urease and trypsin inhibitor activities and improved (P less than .05) the apparent digestibility of amino acids and N in both types of soybeans. However, the heated, conventional soybeans contained more trypsin inhibitor activity than the heated, low-trypsin-inhibitor soybeans and the digestibilities of the amino acids were lower (P less than .05). Although the urease and trypsin inhibitor activities of the two heated soybean sources were similar to or less than those of soybean meal, the digestibilities of amino acids were not as great (P less than .05) in the heated soybeans as in soybean meal.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Apparent digestibility of amino acids in raw and heated conventional and low-trypsin-inhibitor soybeans for pigs. 156 6

Two 21-d trials were conducted to evaluate the effect of heating time and sodium metabisulfite (SMBS) on the nutritional value of full-fat soybeans for chicks. In Trial 1, four pen-replicates of eight chicks each were fed corn-based diets (19% CP; 3,167 kcal of ME/kg) containing either 44% CP soybean meal or full-fat soybeans. The soybeans either were unheated or were autoclaved at 121 degrees C for 10, 20, 30, 40, 60, or 90 min. Soybean oil was added to the soybean meal diet to make it isoenergetic with the soybean diets. Trypsin inhibitor, urease activity, and the solubility of protein in the soybeans decreased as heating time increased. Weight gain increased and feed:gain and pancreas weights decreased quadratically (P less than .01) with heating time. Rate and efficiency of gain were maximized when the soybeans were heated for 40 min; further heating for 60 or 90 min reduced performance. In Trial 2, SMBS was added at levels of 0, 1, or 2% to full-fat, unheated soybeans or to soybeans before autoclaving at 121 degrees C for 10, 20, or 40 min. Four pen-replicates of seven chicks each were fed corn-soybean diets (19% CP; 3,144 kcal of ME/kg) with 12 treatments in a factorial arrangement of heating times and SMBS levels. The rate and efficiency of chick weight gain improved linearly (P less than .01) and pancreas weights decreased linearly (P less than .01) as heating time increased. Less heating time was required to maximize performance and minimize pancreas weights when SMBS was added, resulting in a heating time x SMBS interaction (P less than .05). Under the conditions of this research, chicks fed full-fat soybeans achieved maximum performance when the soybeans were heated at 121 degrees C for 40 min, and SMBS decreased by one-half the heating time required to inactivate the trypsin inhibitors. Trypsin inhibitor activity in soybeans was more closely related to their nutritional value than was urease activity.
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PMID:Effects of heating time and sodium metabisulfite on the nutritional value of full-fat soybeans for chicks. 175 23

The effects of thermal treatment, dry heat and steam on the physiologically active substances: urease and trypsin inhibitors of soybean products, were evaluated by means of urease activity and trypsin inhibitor activity. The parameters time and temperature, moisture and particle size were considered. From these analyses it can be concluded that the best conditions to obtain optimum soybean products were 25% of initial moisture content, exposed to steam (97 degrees C) during four to eight minutes.
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PMID:[Selection of parameters for thermal treatment of soybeans by enzyme inactivation]. 383 74

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

In the present study, three cone openings (0.133; 0.106, and 0.080 cm) and three initial moisture content values (9%, 15% and 21%) were used as treatments to evaluate their effects on the protein quality of full-fat soybean flour, extruded in the Brady Crop Cooker. The specific volume, protein and oil contents as well as available lysine content characteristic of the final product, were not affected by the treatments used. Processing temperatures, however, decreased when the initial moisture content of the material was increased. The nitrogen solubility index was affected by the cone opening but not by the moisture content of the material. With respect to the trypsin inhibitors content, the increase in the initial moisture content in soybeans gave conflicting results. At the 21% moisture treatment, the amounts of trypsin inhibitors were higher than those present in the raw material; a similar effect was also observed with urease activity. At the other two moisture contents (9 and 15%) the amounts of trypsin inhibitors and urease activity were decreased by heat treatment, mainly at the 9% moisture level, which were related to the cone opening of the extruder. PER values in rats were influenced by the moisture content and were not affected by the cone opening. Results obtained in the biological assays with chicks, both for weight gain and conversion efficiency, were favored by a decrease in cone opening. Nevertheless, the increase in the moisture content induced a decrease in weight gain at the 5- and 8-week periods, without affecting the conversion efficiency. The effect of consecutive passes of the material through the extruder was also studied. The product obtained with two extrusions presented a good biological value, probably as a consequence of the low values in the trypsin inhibitors and urease activities. When the material was extruded three times, results proved to be poor, due to a reduction to significant low levels of available lysine content--which becomes limiting--, and nitrogen solubility index of the full-fat soybean flour.
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PMID:Effects of cone opening, initial moisture content and multiple extrusion on the protein quality of extruded soybean using the Brady Crop Cooker. 393 87

Cysteine residues in the active center of jack bean urease [EC 3.5.1.5] were modified with 14C-labeled diazonium-1H-tetrazole (DHT). The labeled enzyme was carboxymethylated with iodoacetic acid, and then hydrolyzed with trypsin. The tryptic digest was subjected to gel filtration on Sephadex G-50, yielding two radioactive fractions. The [14C]DHT-labeled peptide having a lower molecular weight, which was determined to be approximately 1,000 by the method of gel filtration, was further purified to homogeneity by ion-exchange chromatography on DEAE-Sephadex A-25. [14C]DHT-labeled cysteine was identified as cysteic acid after performic acid oxidation, and the amino acid sequence of the low-molecular-weight [14C]DHT-labeled peptide was determined to be Phe-Glu-Pro-Gly-Asp-Cys-Asn-Ser-Thr-Phe-Lys.
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PMID:Amino acid sequence around a cysteine residue in the active center of jack bean urease. 649 Jun 9

Dielectric heating at frequencies of 42 and 2450 MHz was applied to whole soybeans of natural moisture content for varies exposure times. The minimum energy absorbed (MEA) was calculated from moisture-loss and temperature-elevation data. Biochemical analyses were performed to determine protein dispersibility index (PDI), nitrogen solubility index (NSI), and trypsin-inhibitor, urease, lipoxygenase, and peroxidase activities. Because the heating rates were different at the two frequencies for the power levels used, plots of the biochemical properties against temperature of exposure time showed an apparent frequency dependence. This dependence on frequency disappeared, however, when MEA was substituted as the independent variable. Chemical analyses revealed that dielectric heating of soybeans at natural moisture levels should be as effective as conventional steam toasting in reducing trypsin-inhibitor activity. PDI and NSI, but not urease, were suitable indicators of trypsin-inhibitor inactivation by dielectric heating. Lipoxygenase was completely inactivated by the dielectric-heating treatments that gave suitable trypsin-inhibitor inactivation, but peroxidase activity remained relatively high, offering possible advantages for bleaching and improved soy product color.
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PMID:Effects of 42- and 2450-MHz dielectric heating on nutrition-related properties of soybeans. 692 Apr 15

From poly(vinyl alcohol) precursors, various reactive carriers for the immobilization of enzymes were synthesized. As insoluble starting polymers, the following products were used: poly(vinyl alcohol), gels crosslinked with terephthalaldehyde, hydrolyzed beads of crosslinked poly(vinyl acetate), poly(vinyl acetate-co- ethylene) tubes coated with poly(vinyl alcohol), and poly(vinyl alcohol)-containing synthetic pulp. Reactive groups introduced into these carriers or methods for their activation included the diazonium- and isothiocyanato group, and the glutardialdehyde-, BrCN, 2, 4, 6-trichloro-s-triazien, and p-benzoquinone methods. Furthermore, SH-specific reactive groups such as N-substituted maleimide groups or activated mixed disulfides with 2-thiopyridyl groups could be introduced into PVA-polymers. Enzymes like hydrolases (e.g. papain, trypsin, chymotrypsin, urease), oxidoreductases (e.g. glucose oxydase, catalase, glucose-6-phosphate dehydrogenase) as well as the example of transferase hexokinase coimmobilized with glucose-6-phosphate dehydrogenase, were immobilized by reactive poly(vinyl alcohol) carriers. The properties of the immobilized enzymes were investigated.
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PMID:Some new reactive polymers for the immobilization of enzymes. 741 95


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