Sodium cellulose phosphate

Mechanism of Action A nonabsorbable compound that alters urinary composition of calcium, magnesium, phosphate, and oxalate. Calcium binds to cellulose sodium phosphate, thus preventing intestinal absorption of it. Therapeutic Effect Prevents the formation of kidney stones. 

Suspend each dose of cellulose sodium phosphate (CSP) powder in glass of water, soft drink, or fruit juice... 

The client with calcium renal calculi is prescribed cellulose sodium phosphate (Calcibind). The client asks the nurse, How will this medication help prevent my stones from coming back Which statement is the nurse s best response ... 

Poly-O-phosphate, Na salt Cellulose sodium phosphate, USAN. Calcisorb. Calcibind [9038-41-9]... 

Purification of photoprotein. The dialyzed photoprotein solution was centrifuged to remove precipitates, and then subjected to fractional precipitation by ammonium sulfate, taking a fraction precipitated between 30% and 50% saturation. The protein precipitate was dissolved in 50 ml of 10 mM sodium phosphate, pH 6.0, containing 0.1 mM oxine ( pH 6.0 buffer ), dialyzed against the same buffer, and the dialyzed solution was adsorbed on a column of DEAE-cellulose (2.5 x 13 cm) prepared with the pH 6.0 buffer. The elution was done by a stepwise increase of NaCl concentration. The photoprotein was eluted at 0.2-0.25 M NaCl and a cloudy substance (cofactor 1) was eluted at about 0.5 M NaCl. The photoprotein fraction was further purified on a column of Sephadex G-200 or Ultrogel AcA 34 (1.6 x 80 cm) using the pH 6.0 buffer that contained 0.5 M NaCl. 

In the first step, 2.2 g of the ethanol-precipitated solid were dissolved in 55 mL of 0.05M sodium phosphate buffer at pH 7.3, the undissolved residue was removed by centrifugation, and the supernatant was added to a 50-mm i.d., 180-mm long DEAE-cellulose column held at room temperature and eluted with 3.33 mL/min of the same buffer. Since the isoelectric point of the desired xylanase was above the buffer pH, it passed through the column without being retarded, and contaminating protein was removed. 

Electrophoretic Methods. Several electrophoretic procedures have been developed to fractionate or purify the various caseins (McKenzie 1971C Thompson 1971 Whitney 1977). Wake and Baldwin (1961) fractionated whole casein by zone electrophoresis on cellulose powder in 7 M urea and 0.02 ionic strength sodium phosphate buffer at pH 7 and 5°C. Payens and co-workers employed several somewhat different electrophoretic conditions for the fractionation and purification of the caseins on cellulose columns (Payens 1961 Schmidt and Payens 1963 Schmidt 1967). Three fractions, as-, k-, and /3-caseins, were separated at pH 7.5 and 30°C with 4.6 M urea-barbiturate buffer. The purification of asi-casein and the separation of the genetic variants of K-casein were accomplished by altering the electrophoretic conditions. Manson (1965) fractionated acid casein on a starch gel column stabilized by a density gradient at 25 °C. 

Figure 2. Hydrolysis of 14C-cellohexaose (G6) by BS and BI celluloses. The enzymes were purified to homogeneity (3) and incubated with pure uniformly-labeled cellohexaose as described in earlier tests with other celloaextrins (19). Reaction mixtures (0.3 mL) contained 1 mg substrate and cellulose (200 units) in 20mM sodium phosphate, pH 6.2, 0.03% sodium azide. They were incubated at 35°C and at intervals aliquots were removed and chromatographed. Cellodextrins with lower DP (Gt-G5) were located by radioautography and estimated by scintillation spectrometry (19).

It could be shown [5] that the dissolution of polymers depends on the type of ions present in the dissolution medium. Dissolution is base catalyzed and can be described by the Bronstedt dissolution law [38], At a given pH, a linear relationship exists between the logarithm of the dissolution rate and the pKa of the acidic component of the salt present in the dissolution medium. Cellulose acetate phosphate, especially, showed a strong dependency of the dissolution rate on the type of ions added. Sodium chloride prevented the dissolution of some polymers, because the base catalysis was at a minimum level. 

The "mild" NaBH4 reduction was done at 22°C (room temperature) and pH 8.0 The slightly alkaline conditions were necessary to maintain reasonable stability for the NaBH4 reagent. Sodium borohydride, 0.1 mL of 0.25 M NaBH4 in 0.1 M NaOH, was added to test solutions containing 1 mg of cellulose suspended in 0.785 mL of 0.1 M sodium phosphate, pH 8.0 Reaction mixtures were mixed and allowed to react for up to 90 min at room temperature. Reactions were terminated at selected times by the addition of 20 iL of 37% (w/v) HC1. Terminated reaction mixtures were typically allowed to stand for 30 min prior to neutralization by the addition of 95 pL of 2 N NaOH. Separate experiments showed that residual sodium borohydride could not be detected following the low-pH 30-min incubation period. 

Mixed Carbohydrase and Protease, 20 Modified Cellulose, 11 Monoammonium Phosphate, 4 Monobasic Potassium Phosphate, 40 Monobasic Sodium Phosphate, 54 Monopotassium Phosphate, 40 Monosodium Dihydrogen Phosphate, 54 Monosodium Phosphate, 54... 

C. BTI (Sandoz) was further purified by DEAE-Cellulose (DE-52, Whatman, 30 ml) in 0.025 M Tris-HCL (pH 8.00), eluted with a 10 h, 100 ml, 0.0-0.5 M NaCl linear gradient by acid precipitation where the DEAE elutant was dialyzed into 0.05 H sodium acetate (pH 4.5) and the percipitate removed by centrifugation and by Sephadex 6-75 super fine (Pharmacia) gel permeation chromatography (95 x 1.3 cm i.d. column) in 0.025 M sodium phosphate (pH 8.0). Alkaline-dissolved and partially purified 6-endotoxin was analyzed by 12.5% SDS-PAGE (.28), stained with Coomassie brilliant blue (Figure 1). 

Nicotinic acid and nicotinamide and their derivatives were analyzed by TLC on MN 300G cellulose plates in various solvent systems (K. Shibata, personal communications, October 16, 2001). The Rf values of nicotinamide adenine dinucleotide phosphate or NADP" (Rf values 0.03, 0.50, and 0.70), nicotinamide adenine dinucleotide or NAD" (Rf values 0.13, 0.61, and 0.58), nicotinic acid adenine dinucleotide (Rf values 0.15, 0.52, and 0.57), nicotinamide mononucleotide (Rf values 0.11, 0.63, and 0.73), nicotinic acid mononucleotide (Rf values 0.13, 0.47, and 0.75), nicotinamide (Rf values 0.87, 0.88, and 0.45), and nicotinic acid (Rf values 0.77, 0.82, and 0.55) are shown in various solvent systems [1 M ammonium acetate-95 % ethanol (3 7), pH 5.0 2-butyric acid-ammonia-water (66 1.7 33), and 600 g of ammonium sulfate in 0.1 M sodium phosphate-2% 1-propanol (pH 6.8), respectively]. The detection is performed by illumination under short-wavelength (257.3 nm) UV light. Urinary metabolites of the vitamin could be analyzed by TLC. ... 

Purify on DEAE-cellulose, equilibrated with 10 mM sodium phosphate buffer, pH 7.4. Free antibody passes directly, while conjugate can be eluted subsequently with same buffer containing 300 mM KCI. Substitution rate will be about 1.6. 

Abbreviations BA benzyl alcohol BHT butylated hydroxytoluene BKC benzalkonium chloride BzCI benethonium chloride CCS croscarmellose sodium cit citric acid dex dextrose IPM isopropyl myristate KP potassium phosphates MCC microcrystalline cellulose MeC methyl cellulose MePB methyl parabens Mr relative molecular mass NaCit Na citrate NaCMC Na carboxymethylcellulose Na2edta disodium edetate NaP sodium phosphate PEG polyethylene glycol PE-OH phenylethyl alcohol PG propylene glycol pov povidone PrPB propyl parabens SAI steroidal anti-inflammatory Tw Tween (polysorbate)... 

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