Separation of Leucylaminopeptidase Components in Normal Human Sera by DEAE Cellulose Column Chromatography

1962 ◽  
Vol 109 (2) ◽  
pp. 411-412 ◽  
Author(s):  
F. J. Behal ◽  
C. B. Kanavage ◽  
R. D. Hamilton
Keyword(s):  
Column Chromatography ◽  
Deae Cellulose ◽  
Deae Cellulose Column ◽  
Human Sera ◽  
Normal Human ◽  
Cellulose Column

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 Studies on ox brain aminopeptides

1967 ◽  
Vol 105 (2) ◽  
pp. 641-646 ◽  
Author(s):  
A. S. Brecher ◽  
R. E. Sobel
Keyword(s):  
Ammonium Sulphate ◽  
Column Chromatography ◽  
Deae Cellulose ◽  
Deae Cellulose Column ◽  
Cellulose Column ◽  
Inhibited Enzyme

1. Mn2+-inhibited and Mn2+-activated aminopeptidases have been observed in ox brain and separated from one another by DEAE-cellulose column chromatography. 2. The Mn2+-inhibited enzyme has been purified 36-fold; it exhibits a specificity for tripeptide substrates, whereas the Mn2+-activated aminopeptidase cleaves dipeptides as well as tripeptides. 3. Ammonium sulphate treatment generates a Mn2+-stimulated aminopeptidase that is stable to dialysis against EDTA and water, in contrast with an endogenous Mn2+-activated preparation that is irreversibly denatured by such dialysis against EDTA and water.

scholarly journals Studies on tryptophan synthetases from various strains of Bacillus subtilis

1969 ◽  
Vol 112 (3) ◽  
pp. 285-292
Author(s):  
Jerzy W. Meduski ◽  
Stephen Zamenhof
Keyword(s):  
Bacillus Subtilis ◽  
Ammonium Sulphate ◽  
Column Chromatography ◽  
Proteolytic Enzymes ◽  
Deae Cellulose ◽  
Deae Cellulose Column ◽  
Ammonium Sulphate Precipitation ◽  
Tryptophan Synthetase ◽  
Cellulose Column

1. Tryptophan synthetase B of three strains of Bacillus subtilis was prepared from ‘exo-protoplastic’ and ‘endo-protoplastic’ fractions; the enzyme from ‘exo-protoplastic’ fraction was purified 30- to 120-fold by ammonium sulphate precipitation and DEAE-cellulose column chromatography; the latter step separated this enzyme from tryptophan synthetase A, tryptophanase and proteolytic enzymes, but the purified preparations were not stable. 2. The activity of tryptophan synthetase B did not depend on the presence of tryptophan synthetase A. 3. Tryptophan synthetases B of the strains tested differed in their utilization of 2- and 7-methylindole as compared with indole; this suggests that these tryptophan synthetases B are not identical.

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