Cellulose ion-exchanger

Actinia cari. When an extract of the tentacles of this species was subjected to gel nitration, a single protein peak having hemolytic and lethal activities was obtained. Further fractionation by CM-cellulose ion-exchange chromatography yielded three well separated peaks (CTl, Cmi, Cmil) which appeared to be similar in biological activity (14). 

Sensors based on the above reaction scheme have been developed for Al3+, Zn2+, Cu2+, Ca2+, Pb2+, Hg2"1", K+, Li+, etc. A polycation, protamine sensor has also been developed using 2/7/-dichlorofluorescein octadecyl ester (DCFOE) doped in polymer membranes. However, most of these sensors are pH dependent due to the pH dependence of the cation complexation reactions. The cation ion indicators can be immobilized on any solid support, such as silica, cellulose, ion-exchange resin, porous glass, sol-gel, or entrapped in polymer membranes. 

Since the reaction has been reviewed recently (12) only a few additional facts will be mentioned. Many optically active cyanohydrins can be prepared (33) with e.e. s of 84 to 100% by the use of the flavopnotein D-oxynitrilase adsorbed on special (34) cellulose ion-exchange resins. Although the enzyme is stable, permitting the use of a continuously operating column, naturally only one enantiomer, usually the R isomer, is produced in excess. This (reversible) enzyme-catalyzed reaction is very rapid (34). Nonenzymic catalysts, such as the cinchona alkaloids, permit either enantiomer to be prepared in excess. 

Figure 19.9. Chromatogram for stepwise elution of bovine serum albumin on a Vistec diethyl aminoethyl cellulose ion-exchanger, using stepwise increases in sodium chloride concentration in the mobile phase to achieve selective desorption. Proteins 1, serum fraction not adsorbed by column (includes y-gobuhn) 2,3,...

After dissociation of the 70 S ribosome into its two subunits followed by zonal centrifugation for the separation and isolation of the 30 S and 50 S subunits on a preparative scale, the ribosomal proteins were extracted by acetic acid and then separated by cellulose ion exchange chromatography and by gel filtration on Sephadex in the presence of 6 M urea. In this way all the 53 individual ribosomal proteins have been isolated (Wittmann, 1974). Proteins prepared in this manner have been used for physical studies (Brimacombe et al., 1978 Wittmann, 1982) as well as for immunological investigations (Stoffler et al., 1980 Lake,... 

Peterson, E. A. (1970) Cellulosic Ion Exchangers, Elsevier-North Holland, Amsterdam... 

El 3. In what order would the following proteins be eluted from a DEAE-cellulose ion exchanger by an increasing salt gradient. The pHj is listed for each protein. 

DEAE-cellulose ion-exchange chromatography, which is dependent on the phosphate, pyrophosphate or phosphoethanolamine groups of the lipid A moiety, is widely used for lipid A isolation (El Hamidi et al., 2005 Raetz and Kennedy, 1973). TLC, as a lipids detection method, also can be applied for lipid A isolation (Zhou et al., 1999). In addition, the chromatography techniques based on the molecular... 

Since these earlier studies a variety of different methods and techniques have appeared for purifications of the serum transferrins. Precipitation of human serum transferrin by rivanol appears to have been used widely as an initial purification step (17, 18, 80, 107). A method for the preparation of large quantities of human serum transferrin was proposed by Inman et al. (69). The Inman method employed solvent and salt fractionation and cellulose ion exchange chromatography. A number of other workers have used cellulose ion exchange chromatography in combination with other procedures, such as electrophoresis (14, 22, 57, 105, 112, 137). 

Silica gel can also be used as a solid support on which liquids are immobilized to produce LLC systems. Most common are nonpolar phases for reverse phase work. Other chemicals used as stationary phases include cellulose and cellulose ion exchangers, polyamide, magnesium oxide, and Kieselguhr. Silver nitrate is added to silica gel to retain olefins selectively, as noted earlier. The review by Scott15 can be consulted for further information on the stationary phase in TLC. 

Amino acid composition of the serum proteins. II. Fractionation of human serum proteins by cellulose ion-exchange chromatography and comparative amino acid composition of the fractions. Ibid., 19, 451 (1958). With S. Keller. 

Chemical relationship between the protein fractions obtained from fowl serum by cellulose ion-exchange chromatography. Evidence for amino acid anlage. Arch. Biochem. Biophys., 83, 426 (1959). With S. Keller and D. W. Meller. 

In 1965, Yonetani and Ray (14) obtained a highly purified preparation of cytochrome c peroxidase in an excellent yield using DElAE-cellulose ion exchange chromatography. Shortly thereafter, Yonetani et al. (15) crystallized this enzyme by isoelectric dialysis. Subsequently, Yonetani and co-workers (16-40) carried out a series of extensive investigations... 

E. A. Peterson, Cellulosic Ion Exchangers, American Elsevier, New York, 1970. 

Cellulose ion-exchange materials and layers of cellulose which have... 

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