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.

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

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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