scholarly journals Role of neuraminic acid in the heterogeneity of alkaline phosphatase in sheep brain

1968 ◽  
Vol 107 (2) ◽  
pp. 185-190 ◽  
Author(s):  
S. Saraswathi ◽  
B. K. Bachhawat
Keyword(s):  
Alkaline Phosphatase ◽  
Deae Cellulose ◽  
Acetylneuraminic Acid ◽  
Deae Cellulose Column ◽  
Elution Pattern ◽  
Sheep Brain ◽  
Substrate Affinities ◽  
Enzyme I ◽  
Cellulose Column

1. Two alkaline phosphatase fractions from sheep brain obtained by DEAE-cellulose column chromatography were shown to be associated with different concentrations of NANA (N-acetylneuraminic acid). Enzyme II contains nearly three times as much NANA as does enzyme I. 2. Partial removal of NANA by neuraminidase digestion from these alkaline phosphatase fractions has different effects on their chromatographic properties. Though the enzymic release of NANA has no effect on the elution pattern of enzyme I from a DEAE-cellulose column, such a treatment shifts the elution pattern of enzyme II towards that of enzyme I. 3. However, this change in the elution pattern of enzyme II as a result of the removal of NANA does not produce any change in the kinetics of this fraction, and the differences between enzyme I and enzyme II with respect to their substrate affinities and Ki for phosphate inhibition are maintained even after the removal of NANA. 4. Results indicate that NANA is not the only factor responsible for the heterogeneity of alkaline phosphatase in sheep brain and enzyme I is not the result of the removal of NANA from enzyme II.

scholarly journals Alkaline phosphatase from pig kidney. Microheterogeneity and the role of neuraminic acid

1974 ◽  
Vol 141 (1) ◽  
pp. 293-298 ◽  
Author(s):  
Kunio Hiwada ◽  
Ernst D. Wachsmuth
Keyword(s):  
Alkaline Phosphatase ◽  
Brush Border Membrane ◽  
Deae Cellulose ◽  
Multiple Forms ◽  
Alkaline Phosphatases ◽  
Acetylneuraminic Acid ◽  
Pig Kidney ◽  
Ph Dependency ◽  
Polypeptide Chains

Several alkaline phosphatases (EC 3.1.3.1) could be obtained from pig kidney brush-border membrane on extraction with butan-1-ol. Three of the multiple forms were separated by DEAE-cellulose chromatography and further purified. They form a regular series with different degrees of glycosylation (mainly owing to N-acetylneuraminic acid), of charge, of molecular weight, of stability to temperature, to pH and to urea, of minimal requirement for Mg2+ and of extractability by butan-1-ol. In contrast, the detectable antigenic sites, the inhibition by amino acids and the pH-dependency of Km and Vmax. were identical for these multiple forms. On treatment with neuraminidase, the multiple forms became identical in all their properties. It was therefore concluded that the microheterogeneity of alkaline phosphatase is due to different degrees of glycosylation at polypeptide chains which appear to be otherwise identical.

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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