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.

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.

SEPARATION OF AN α-GALACTOSIDASE FROM WATERMELON SEEDS

1964 ◽  
Vol 42 (5) ◽  
pp. 605-612 ◽  
Author(s):  
Moin Uddin Ahmed ◽  
F. S. Cook
Keyword(s):  
Ammonium Sulphate ◽  
Deae Cellulose ◽  
Ph Optimum ◽  
Deae Cellulose Column ◽  
Ammonium Sulphate Precipitation ◽  
Cellulose Column

An α-galactosidase from watermelon seeds has been separated from invertase and β-galactosidase by ammonium sulphate precipitation followed by elution from a DEAE-cellulose column with phosphate buffers. This enzyme is capable of hydrolyzing galactose residues from melibiose, raffinose, and stachyose. The pH optimum with the three substrates is close to 4.2. The enzyme is inhibited by the products of the reaction, and, in the case of melibiose, by the substrate itself.

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
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