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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The principles and practice of nitrosamine degradation by photochemical means were described. Two types of apparatus were constructed for this purpose. A nitrosamine waste solution containing 10-3-10-1 N in hydrochloric acid and about 10 mole-equivalents of an HNO2 scavenger (i.e., urea, guanidine, or hydrazoic acid) was efficiently and irreversibly degraded to the parent amines and N2 (and/or N2O) by irradiation. Efficiency of the degradation depended on the type of apparatus used. With the use of one apparatus, about 11 g N-nitrosodimethylamine was photolytically converted to dimethylamine, N2, and N2O in 24 hours. Protonated guanidine catalyzed the photohydrolysis processes.
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PMID:Efficient photolytic degradation of nitrosamines. 99 11

A method has been developed for the purification of beta-cyano-L-alanine synthase from etiolated 10-day-old seedlings of blue lupine. High purity preparations of the enzyme were obtained with specific activity exceeding 4000-fold that of the seedling homogenate. Preparations were homogeneous on electrophoresis in polyacrylamide gel. The yield of total activity after purification was approximately 20%. Glutamic acid is the enzyme's only N-terminal amino acid; the molecular weight of the enzyme (both native and treated with 6 M urea) is 52000. The synthase containes one mole of pyridoxal-P per mole of protein; its isoelectric point is situated at pH 4,8. The enzyme's absorption spectrum has a maximum at 410 nm i.e., in the characteristic range of many pyridoxal-U-containing enzymes. Data on the amino acid composition of the enzyme are presented.
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PMID:[Beta-cyanoalanine synthase: Its purification and basic physico-chemical properties]. 103 Jun 42

The erythroblastic leukemia produced in Long-Evans rats by the administration of 7, 8, 12 trimethylbenz (a) anthracene has been used as a model of the most immature form of the erythrocyte series. In conjunction with studies of the maturation of several other membrane functions, the permeability of this cell to water and to certain definitive non-electrolytes was measured with osmotic methods. The hydraulic conductivity, L-p was 6.2 micro (minute)-1, (atm)-1 at 25 degrees C, quite high and characteristic of mature erythrocytes, but different from values of 0.65 for immature myeloid cells. The effect of temperature provided an energy of activation of 4.4 kCal/mole, also typical of mature mammalian erythrocytes but again different from 13 to 18 kCal/mole for immature myeloid cells. Urea was compared to thiourea. The permeability coefficient for urea was 76.7 micra (minute)-1 plus or minus 13.8 (S. E.); the value for thiourea was 1.55 micra (minute)-1 plus or minus 0.18 (S. E.). Phloretin at 0.25 mM inhibited urea permeability by 90% with 50% inhibition occurring at 0.05 mM. Inhibition was reversible. Permeability to the glycols was also compatible with mature erythrocytes. We infer from these findings that the structure which underlies these basic, passive membrane functions is laid down early and persists after loss of nucleus and subsequent maturation.
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PMID:Maturation of membrane function: the permeability of the rat erythroblastic leukemic cell to water and to non-electrolytes. 105 96

1. Individual capillaries of the transilluminated frog mesentery have been perfused with suspensions of human red cells in frog Ringer solution containing 1-0 g albumin 100 ml.-1. The outer surface of the mesentery has been washed with normal frog Ringer solution and with frog Ringer solutions made hypertonic by addition of one of the following solutes: sodium chloride (100 m-mole. 1.-1); urea (100 m-mole.1.-1); sucrose (20-50 m-mole. 1.-1); cyanocobalamin (8-5 m-mole. 1.-1). The temperature of the mesentery was between 14 and 16 degrees C in all experiments. 2. Wtih the mesentery superfused with normal Ringer, the filtration coefficient was determined from measurements of the rate of fluid filtration across the capillary wall, at a series of known capillary pressures (Michel, Mason, Curry & Tooke, 1974). Filtration coefficient varied from 0-69 X 10(-3) to 4-45 X 10(-3) mum. sec-1 .cm H2O-1 with an average value of 1-87 X 10(-3) mum. sec-1. cm H2O-1. 3. When the superfusate was made hypertonic by the addition of a test solute, the osmotic reflextion coefficient (sigma) of the capillary wall to test solute was calculated from the additional rate of filtration, the concentration of test solute in the superfusate and the filtration coefficient. Average values for sigma were: sodium chloride, 0-068 +/- 0-03 (three capillaries); urea, 0-071 +/- 0.015 (four capillaries); sucrose, 0-115 +/- 0-023 (seven capillaries); cyanocobalamin, 0-100 +/- 0-03 (three capillaries). 4. In further experiments, the osmotic reflextion coefficients to sodium chloride, urea and sucrose were determined in the same capillary. Five technically acceptable experiments were carried out. Although there were differences in the value of sigma between different capillaries, in any one capillary values of sigma were of the same magnitude and there appeared to be no significant trend with the molecular size of the test solute. 5. Our findings are inconsistent with the hypothesis that there is a single pathway for water and small hydrophilic molecules across the capillary wall. 6. Our results may be interpreted in terms of an exclusive channel for water in parallel with a channel shared by both water and small hydrophilic molecules. It is suggested that the exclusive water channel may be the membranes and cytoplasm of the endothelial cells and the shared channel may be located in the intercellular junctions. 7. Our data suggest the exclusive water channel represents about 10% of the total filtration coefficient in frog mesenteric capillaries. The shared channel shows relatively little restriction to the molecules investigated. Estimates of the volume flow throught the two channels are made for conditions where hydrostatic pressure differences and osmotic pressure differences are the driving forces.
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PMID:Osmotic reflextion coefficients of capillary walls to low molecular weight hydrophilic solutes measured in single perfused capillaries of the frog mesentery. 108 61

Human urinary kallikrein [EC 3.4.21.8] (HUK) was purified about 200-fold with an overall yield of 40 percent from crude powder by DEAE-cellulose chromatography, acetone fractionation, Sephadex G-100 gel filtration and DEAE-Sephadex A-50 chromatography. Its activity was 200 kallikrein units (KU) per A280. HUK from active fractions obtained by DEAE-Sephadex A-50 chromatography was separated into three active components showing isoelectric points of 3.9 (HUK-1), 4.0 (HUK-2), and 4.2 (HUK-3) by isoelectric focusing: each HUK component was homogeneous on disc electrophoresis. The approximate molecular weights of HUK-1, -2 and -3 were estimated to be 2.7 X 10(4), 2.7 X 10(4), and 2.9 X 10(4), respectively, by gel filtration on a Sephadex G-100 column. The optimum pH's of HUK-1, -2, and -3 in esterolytic action were found to be 8.0, 8.3, and 7.5, respectively, and they were fairly heat stable in comparison with other glandular kallikreins. The three components of HUK were weakly inhibited by Trasylol, but were not affected by soybean and ovomucoid trypsin inhibitors. They were strongly resistant to treatment with urea and weakly resistant to treatment with guanidine. The activation energies of HUK-1, -2, and -3 were found to by 1.17 X 10(4), 5.1 X 10(3), and 1.45 X 10(4) cal per mole, respectively. The Km values were estimated toward N-alpha-tosyl-L-arginine methyl ester (TAME), N-alpha-benozyl-L-arginine ethyl ester (BAEE), and N-alpha-benozyl-L-arginine methyl ester (BAME).
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PMID:Studies on urinary kallikreins. I. Purification and characterization of human urinary kallikreins. 108 37

The effect of temperature on the permeability of nonelectrolytes across liposomal membranes above and below their transition temperature has been studied by using an osmotic method. Below their transition temperature, liposomes are osmotically insensitive structures but, on addition of gramicidin A, the water permeability so increased that the permeability of solutes could be studied. The measured activation energies for permeation of a variety of nonelectrolytes has been found to increase when a) there is an increase in the capability of the solutes to form hydrogen bonds in water, b) the cholesterol concentration in the membranes increases and c) the membranes pass from a liquid-crystalline to a solid-crystalline state. The change in the activation energy for permeation per hydrogen bond is about 1.8 kcal/mole for all the different liposome systems investigated; the only solute tested that deviated from this correlation was urea, whose activation energy for permeation across a gramicidin-containing system was much lower than expected from its hydrogen-bonding capacity. This finding suggests that urea is permeating across the gramicidin pore. Although the literature contains only incomplete data relating the activation energies for permeation of nonelectrolytes across biological membranes to their hydrogen-bonding capacity, the available evidence suggests that there is a similar correlation to that found in liposomes. Thus, the average increase in the activation energy per hydrogen bond for permeation across ox red cell membranes (Jacobs, Glassman & Parpart, J. Cell. Comp. Physiol. 7:197, 1935) is 2.2 plus or minus 0.4 kcal/mole, a value that is similar to that obtained in liposomes. However, the activation energies for water and urea are - in such a system - very much lower than expected, suggesting that they, too, are permeating by some parallel route such as an aqueous pore.
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PMID:The permeability of liposomes to nonelectrolytes. I. Activation energies for permeation. 117 Mar 32

The inhibition by some thiol reagents of partly purified mitochondrial monoamine oxidase (MAO) (EC 1.4.3.4) from rat liver was studied, and the molar content of sulfhydryl groups in the enzyme determined. Sodium nitroprusside and 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) inhibited the enzyme, apparently reversibly, while sodium arsenite was not inhibitory. Concentrations of the respective inhibitors causing 50% inhibition after 15 min of preincubation with the enzyme at pH 7.0 and 37 degrees C are 5.80 times 10(-4) M and 4.35 times 10(-5) M. The thiol compounds cysteine, dithiothreitol, and 2-mercaptoethanol did not inhibit MAO. The average number of sulfhydryl groups per mole of enzyme, determined by reaction with DTNB, increased from 3.6 +/- 0.2 freely reacting sulfhydryl groups (n = 4) to 18.4 to total sulfhydryl groups (n = 2) on denaturation with 8 M urea.
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PMID:Essential sulfhydryl groups of rat liver monoamine oxidase. 118 Oct 10

Ruminal fermentation and disappearance of glucose, starch, and cellulose, and incorporation of glucose and starch into microbial cells were estimated in a fistulated Jersey cow fed twice daily a purified diet containing urea as the sole nitrogen source. Estimated rumen volume was 59.8 liters. Turnover time and rate of passage of rumen contents were 33.4 h and 1.8 liters per h. Turnover times of glucose, starch, and cellulose were .17, 4.7, and 14.2 h. Fermentation times of glucose, starch, and cellulose were .17, 5.5, and 25.1 h. Percentages of glucose, starch, and cellulose utilized in the rumen were 99.4, 85.4, and 60.6. Thus, 18.5% of the carbohydrate fed bypassed rumen fermentation, and 81.5% was utilized in the rumen. All glucose disappeared from the rumen within an hour. An average of 32.1, 43.0, and 14%, respectively, of glucose utilized was incorporated into microbial cells, volatile fatty acids, and carbon dioxide. Percentage of starch incorporated into cells varied, with time being highest 2 h after feeding at 40% and lowest at 20%, 10 h after feeding. Respective percentages of starch incorporated into microbial cells, volatile fatty acids, and carbon dioxide were 32.4, 45.9; and 13.3. Total microbial protein and cell yields per kilogram carbohydrate utilized in the rumen were 77.1 and 117.5 g. Microbial cell yield per mole (estimated) of adenosine triphosphate was 16.2 g.
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PMID:Dynamics of fermentation of a purified diet and microbial growth in the rumen. 126 77

Washed cell suspensions of mixed rumen bacteria were used to evaluate effects of 100% urea-nitrogen and 75% urea-nitrogen plus 25% amino acid-nitrogen in growth media upon microbial growth rate and yield, specific rate of glucose consumption, and incorporation of glucose into mixed cells, carbon dioxide, and end products. Rumen microbial dry matter, nitrogen, ribonucleic acid, deoxyribonucleic acid, glucose disappearance, and production of volatile fatty acids were considerably higher in medium containing urea plus amino acids as compared with urea only. Specific growth rates of microbes were .104 and .203 and mean doubling times were 6.7 and 3.4 h in the urea and urea plus amino acid growth media. Microbial growth in mg per 100 mg glucose used, per mole glucose and per mole adenosine triphosphate (ATP), and specific rate of glucose consumption in mmol per mg cells-h were 19.3, 34.7, 15.4, and .016 with urea, and 24.4, 44.2, 20.6, and .014 with urea plus amino acids. Percentages of catabolized glucose incorporated into microbial cells, carbon dioxide, and end products did not differ between treatments and averaged 19.5, 7.8, and 64.4%.
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PMID:Factors influencing rumen microbial growth rates and yields: effects of urea and amino acids over time. 126 78

Effects of isonitrogenous urea and amino acid additions upon microbial growth in rumen contents from a cow fed a purified diet in which urea was the sole nitrogen source were studied. Incorporation of amino acids into microbial cells, volatile fatty acids, and carbon dioxide was estimated. Rates of microbial growth, volatile fatty acid production, and effects of amino acids upon microbial nitrogen yields were highest right after feeding and decreased with time after feeding. Microbial growth and amounts of amino acids incorporated into microbial cells, volatile fatty acids and carbon dioxide were related closely to quantity of starch remaining in the rumen. High amounts of starch increased microbial protein synthesis from carbon-14 labeled amino acids and reduced amounts of amino acid fermentation. Estimated microbial protein yields per day were 326.0, 444.4, 497.3, and 527.3 g when 0, 15, 30, and 45 mg amino acid nitrogen replaced urea nitrogen during incubation. Respective values for microbial cells per mole estimated adenosine triphosphate were 15.2, 19.2, 21.0, and 24.5. Microbial cell yields per kg carbohydrate digested were 139.0, 189.5, 212.0, and 224.8 g for 0, 15, 30, and 45 mg amino acid nitrogen. Addition of small amounts of amino acids to a diet containing urea as the sole nitrogen source improved considerably rumen microbial protein yields.
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PMID:Factors influencing rumen microbial growth rates and yields: effect of amino acid additions to a purified diet with nitrogen from urea. 126 79


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