scholarly journals Bacterial degradation of N-cyclopropylmelamine. The steps to ring cleavage

1984 ◽  
Vol 222 (2) ◽  
pp. 315-320 ◽  
Author(s):  
A M Cook ◽  
H Grossenbacher ◽  
R Hütter
Keyword(s):  
Cyanuric Acid ◽  
Deae Cellulose ◽  
Bacterial Degradation ◽  
Ring Cleavage ◽  
Pseudomonas Spp ◽  
Deae Cellulose Column ◽  
Cell Extracts ◽  
Specific Activities ◽  
Substrate Proteins ◽  
Cellulose Column

The s-triazine cyclopropylmelamine (N-cyclopropyl-1,3,5-triazine-2,4,6-triamine) was degraded to about 6 mol of NH4+/mol of substrate by a mixture of two bacteria (strains A and D, both Pseudomonas spp.) Only strain A grew with cyclopropylmelamine as sole and limiting source of nitrogen. The organism obtained 2 mol of nitrogen/mol of substrate and excreted a product that was identified as cyclopropylammelide [6-cyclopropylamino-1,3,5-triazine-2,4(1 H,3 H)-dione]. Proteins in extracts from strain A were separated on a Sephadex G-200 column. Cyclopropylmelamine was found to be deaminated in two separable steps to cyclopropylammelide via cyclopropylammeline [4-amino-6-cyclopropylamino-1,3,5-triazine-2(1 H)-one], which was identified. Strain D could not utilize cyclopropylmelamine or cyclopropylammeline, but could utilize cyclopropylammelide (or homologue) as sole and limiting source of nitrogen and obtain about 4 mol of nitrogen/mol of substrate. Proteins in cell extracts from strain D were separated on a DEAE-cellulose column. Alkylammelides were degraded quantitatively by one enzyme fraction to 1 mol of cyanuric acid plus 1 mol of alkylamine/mol of substrate. The specific activities of enzymes in extracts of the two strains were as high as the activities observed during growth. The three activities studied in the two strains were all active under aerobic and oxygen-free conditions. The reactions appear to be hydrolytic, yielding 2 mol of NH4+ plus 1 mol of cyclopropylamine and 1 mol of cyanuric acid/mol of substrate.

scholarly journals The degradative pathway of the s-triazine melamine. The steps to ring cleavage

1982 ◽  
Vol 208 (3) ◽  
pp. 679-684 ◽  
Author(s):  
K Jutzi ◽  
A M Cook ◽  
R Hütter
Keyword(s):  
Enzyme Preparation ◽  
Cyanuric Acid ◽  
Deae Cellulose ◽  
Sole Source ◽  
Ring Cleavage ◽  
Pseudomonas Sp ◽  
Degradative Pathway ◽  
Degradative Enzymes ◽  
Specific Activities ◽  
Transient Intermediate

1. The degradative pathway of melamine (1,3,5-triazine-2,4,6-triamine) was examined in Pseudomonas sp. strain A. 2. The bacterium grew with melamine, ammeline, ammelide, cyanuric acid or NH+4 as sole source of nitrogen, and each substrate was entirely metabolized. Utilization of ammeline, ammelide, cyanuric acid or NH+4 was concomitant with growth. But with melamine as substrate, a transient intermediate was detected, which was identified as ammeline by three methods. 3. Enzymes from strain A were separated by chromatography on DEAE-cellulose, and four activities were examined. 4. Melamine was converted stoichiometrically into equimolar amounts of ammeline and NH+4. 5. Ammeline was converted stoichiometrically into equimolar amounts of ammelide and NH+4; ammelide was identified by four methods. 6. Ammelide was converted stoichiometrically into equimolar amounts of cyanuric acid and NH+4; cyanuric acid was identified by four methods. 7. Cyanuric acid was converted by an enzyme preparation into an unidentified product with negligible release of NH+4. 8. The specific activities of the degradative enzymes (greater than or equal to 0.3 mkat/kg of protein) were high enough to explain the growth rate of the organism. 9. The bacterium converted 0.4 mM-melamine anaerobically into 2.3 mM-NH+4. 10. Two other pseudomonads and two strains of Klebsiella pneumoniae were also examined, with similar results. 11. The degradative pathway of melamine appears to be hydrolytic, and proceeds by three successive deaminations to cyanuric acid, which is further metabolized.

A simple assay for galactokinase using deae-cellulose column chromatography

1977 ◽  
Vol 74 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Y.S. Shin-Buehring ◽  
M. Osang ◽  
R. Ziegler ◽  
J. Schaub
Keyword(s):  
Column Chromatography ◽  
Deae Cellulose ◽  
Deae Cellulose Column ◽  
Cellulose Column

scholarly journals Leaf proteins in five varieties of red clover cultivated in Poland

2015 ◽  
Vol 26 (2) ◽  
pp. 213-216 ◽  
Author(s):  
W. Maciejewska-Potapczyk ◽  
L. Konopska ◽  
K. Bytniewska ◽  
A. Radziwonowska ◽  
H. Zawierucha ◽  
...  
Keyword(s):  
Total Protein ◽  
Deae Cellulose ◽  
Red Clover ◽  
Protein Fractions ◽  
Leaf Proteins ◽  
Deae Cellulose Column ◽  
Globulin Level ◽  
Cellulose Column

Protein fractions: albumins, globulins, gluteins and prolamins were extracted from the leaves of 5 varieties of red clover. 'Skrzeszowicka' and 'Hruszowska' showed the highest content of total protein, 'Rotra' however – the highest globulin level. Globulins were fractionated on DEAE cellulose column into 3 fractions. Globulins from 'Rotra' and 'Hruszowska' varieties were separated into 4 fractions.

Extracellular nuclease produced by a marine bacterium. II. Purification and properties of extracellular nuclease from a marine Vibrio sp.

1976 ◽  
Vol 22 (10) ◽  
pp. 1443-1452 ◽  
Author(s):  
M. Maeda ◽  
N. Taga
Keyword(s):  
Enzyme Activity ◽  
Deae Cellulose ◽  
Strong Stability ◽  
Rnase Activity ◽  
Salting Out ◽  
Deae Cellulose Column ◽  
Marine Vibrio ◽  
Extracellular Nuclease ◽  
Marine Vibrio Sp ◽  
Cellulose Column

Extracellular nuclease produced by a marine Vibrio sp., strain No. 2, was purified by salting out with ammonium sulfate and by chromatography on a DEAE-cellulose column and twice on a Sephadex G-200 column. The nuclease was eluted as a single peak in which the deoxyribonuclease (DNase) activity and ribonuclease (RNase) activity appeared together. Polyacrylamide disc gel electrophoresis showed a single band of stained protein which had both DNase and RNase activity. The molecular weight of the enzyme was estimated to be 100 000 daltons. When using partially purified enzyme from the DEAE-cellulose column, the optimum pH for activity was 8.0, and the enzyme was activated strongly by 0.05 M Mg2+ ion and stabilized by 0.01 M Ca2+ ion. These concentrations of Mg2+ and Ca2+ ions are similar to those of the two cations in seawater. Indeed, the enzyme revealed high activity and strong stability when kept in seawater. The presence of particulate matter, such as cellulose powder, chitin powder, Hyflosupercel, Kaolin, and marine mud increased the stability of the enzyme. When the hydrostatic pressure was increased from 1 to 1000 atmospheres, the decrements of the enzyme activity were more pronounced at 30 and 40 °C than at 25 or 50 °C. The enzyme activity was restored after decompression to 1 atm at 30 °C.

scholarly journals Separation of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase activities

1978 ◽  
Vol 171 (3) ◽  
pp. 659-663 ◽  
Author(s):  
R H Tukey ◽  
R E Billings ◽  
T R Tephly
Keyword(s):  
Deae Cellulose ◽  
The Other ◽  
Rabbit Liver ◽  
Transferase Activity ◽  
Deae Cellulose Column ◽  
Cellulose Column

Rabbit liver UDP-glucuronyltransferase activity was resolved into two separate fractions on DEAE-cellulose, one containing most of the transferase activity toward oestrone and the other most of the activity toward p-nitrophenol. These two activities were completely separated by rechromatography of each fraction on a second DEAE-cellulose column.

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