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Applications:
ION EXCHANGE
- PERLCELLULOSE - EIN NEUER MAKROPORÖSER TRÄGER FÜR IONENAUSTAUSCHER UND
ANALOGE SYSTEME
- Stamberg J., Peska J., Paul D., Philipp B.: Acta
Polymerica, 30 (1979) 734-739
Based on various principles of preparing cellulose particles for ion exchangers a
technique of preparation of spheric cellulose particles having narrow pore size
distribution is described. With respect to the morphological parameters the properties of
the pearl cellulose thus obtained are characterized. Various possibilities of subsequent
modification of the chemical and morphological structure are considered. With some
selected examples the large field of possible application of pearl cellulose is outlined.
- SORPTION OF GOLD ON SPHERICAL CELLULOSE-BASED WEAKLY BASIC ANION EXCHANGER
(Iontosorb DEAE)
- Dubsky F., Cernajova V.: Scientific Papers
of the Prague Institue of Chemical Technology, H 18
(1983) 137-145
The sorption of gold and of four common metals (copper, nickel, cobalt and iron) was
studies on two types of spherical cellulose anion exchangers involving diethylaminoethyl
functional groups (Iontosorb DEAE). Gold was found to be sorbed selectively from dilute
hydrochloric acid, of which use was made for its separation from excess common metals.
- BEAD CELLULOSE ANION EXCHANGERS FOR ULTRA PURE WATER (Iontosorb DEAE, Iontosorb TMAHP)
- Matejka Z.: Effluent and Water Treatment
J., 275 (1984)
The ability and efficiency of bead cellulose anion exchangers to take up higher
molecular weight humic acids were investigated. Equilibrium sorption and desorption tests,
comparative dynamic (columns) runs with styrene and cellulose resins analog with
gel-chromatography analysis of the raw and treated water proved the suitability of the
bead cellulose resins to act as a simple and cheap substitute for clarification in the
production of ultra pure water.
- COMPETITIVE ELUTION OF LACTATE DEHYDROGENASE FROM CIBACRON BLUE-BEAD CELLULOSE
WITH CIBACRON BLUE-DEXTRANS (Iontosorb DEAE)
- Mislovicova D., Gemeiner P., Stratilova E.: J.
Chromatogr., 510 (1990) 197-204
The efficiencies of elution of lactate dehydrogenase (LDH) from Cibacron Blue
(CB)-bead cellulose with eluents ensuring competitive (Cibacron Blue-dextran), biomimetic
(NADH) and displacing (KCl) mechanisms were compared. Competitive elution with CB-dextran
T 10 was shown to be the most effective providing a 38 fold purified enzyme in 83 % yield.
As shown by fast protein liquid chromatography and polyacrylamide gel electrophoresis,
this LDH preparation was free from protein contaminants but contained CB-dextran.
CB-dextran was then removed by ion-exchange chromatography (Iontosorb DEAE) and the yield
of LDH decreased to 62 %. When using a longer column, the enzyme was resolved partially in
two fractions. The isoelectric point of the main fraction was 7.3.
- ISOLATION AND CHARACTERIZATION OF THE PROTEOLYTIC ENZYMES OF CARP HEPATOPANCREAS
(Iontosorb DEAE)
- Kminkova M., Moucka Z., Kucera J.: Potrav.
Vìdy, 15 (1997) 351-362
Proteolytic enzymes (trypsin, chymotrypsin, aminopeptidase and carboxypeptidase A and
B) were separated from carp hepatopancreas, purified and partially characterized.
Aminopeptidase was separated from other enzymes by gel chromatography on Sephadex G-100
(this enzym is an object of our next study). Chymotrypsin and trypsin were separated to
two active components (chymotrypsin I and II and trypsin I and II) by ion exchange
chromatography on DEAE-bead cellulose (Iontosorb DEAE). Trypsin I and chymotrypsin I were
not adsorbed on this sorbent in contrast with trypsin II and chymotrypsin II, which were
eluted from the column with NaCl gradient. Isoeletric points, optimum temperature and pH
were determined for chymotrypsin I and II, trypsin I and II and carboxypeptidase A and B.
The carp enzymes had similar properties to those of other water animals.
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