Sodium phosphate secondary

J. J. Berzelips prepared crystals of tetrahydrated sodium ammonium hydro phosphate, Na(NH4)HP04.4H20, in 1816, by cooling a hot aq, soln. of five parts secondary sodium phosphate, Na2HP04.12H20, with two of the corresponding... 

Synonyms Disodium orthophosphate, Disodium phosphate, DSP, Secondary sodium phosphate. 

The solution will have a very strong alkaline reaction, since it contains a large fraction of 1 mole each of ionized NaOH and of ionized secondary sodium phosphate, Na2HPC>4. The OH- ions thus formed check the hydrolysis of the secondary sodium phosphate but if solid secondary sodium phosphate is dissolved in water, hydrolysis of this salt ensues to a sufficient extent to make the solution alkaline to litmus. 

The most important of the double salts of phosphoric acid with ammonium and the alkali-metals is sodium ammonium hydrogen phosphate or microcosmic salt, NaNH4HP04,4H20, a constituent of putrefying urine, and also present in guano under the name stercorite.17 It can be prepared by the interaction of secondary sodium phosphate and ammonium chloride, or that of secondary ammonium phosphate and sodium chloride. It forms colourless columnar crystals belonging... 

Disodium hydrogen phosphate disodium phosphate E339 phosphoric acid, disodium salt secondary sodium phosphate sodium orthophosphate. 

These terms are also used to name salts of ortho-phosphoric acid (H3P04) in which one, two, or three of the hydrogen atoms have been replaced by metal or radicals NaH2P04 is primary sodium phosphate, Na2HPC)4is secondary sodium phosphate. The same system of names is used for salts of other acids containing three replaceable hydrogen atoms. 

The three salts are also known by a number of other names, such as NaH2P04 primary sodium phosphate, primary sodium orthophosphate, sodium biphosphate, MSP Na2HP04 secondary sodium phosphate, secondary sodium orthophosphate,... 

Teichert et al. [45] were the first to carry out TLC of amines. The hydrochlorides were dissolved in 70% alcohol and applied in 1 to 10 [xg amounts. The hi /-values and experimental conditions for the separation are summarised in Table 94. As can be seen from the table, only a partial improvement in separation is achieved by buffering silica gel G layers with a mixture of 0.2M primary potassium phosphate and 0.2 M secondary sodium phosphate (1 -h 1) or with 0.15M sodium acetate solution. 

I = Silica gel G layer, buffered to pH 6.8 (25 g silica gel G slurried with 50 ml of a mixture of equal amounts of 0.2 M primary potassium phosphate and 0.2M secondary sodium phosphate solutions). Chloroform-96% ethanol (90 + 10) as solvent. 

Pig. 4. CD spectra in the near and far UV of apo- and heme-hemopexin. The CD spectra of rabbit apo- and heme-hemopexin (solid line and dashed line, respectively) at pH 7.4 in 0.05 M sodium phosphate buffer are shown. The increases in ellipticity in the near UV are attributable to changes in tertiary conformation leading to altered environments of aromatic residues, particularly tryptophan. The unusual positive ellipticity in the far UV is attributable to tryptophan-tryptophan interactions that are perturbed by heme binding 124, 130). This positive signal precludes analysis of the secondary structure of hemopexin using current CD-based algorithms. 

Substitution therapy for deficiency states acute or chronic adrenal insufficiency, congenital adrenal hyperplasia, and adrenal insufficiency secondary to pituitary insufficiency, nonendocrine disorders arthritis rheumatic carditis allergic, collagen, intestinal tract, liver, ocular, renal, shin diseases bronchial asthma cerebral edema malignancies PO 5-60 mg/day in divided doses. Intra-articular, Intralesional (acetate) 4-100 mg, repeated as needed. Intra-articular, Intralesional (sodium phosphate) 2-30 mg, repeated at 3-day to 3-week intervals, as needed. IM (acetate, sodium phosphate) 4-60 mg a day. 

Dissolve a hydrazide-containing enzyme or other protein at a concentration of 10 mg/ml in 0.1 M sodium phosphate, 0.15 M NaCl, pH 7.2. For the preparation of a hydrazide-activated enzyme see Chapter 16, Section 2.4. For modification with a hydrazide-containing probe, such as biotin-hydrazide, use a concentration of 5 mM in the phosphate buffer. For conjugation through the amine groups of a secondary molecule, dissolve the amine-containing protein at 10 mg/ml in 0.2 M sodium carbonate, pH 9.6. 

The sections are rinsed in the same buffer and incubated for 90 min in secondary antiserum (Jackson ImmunoResearch Laboratories, West Grove, PA), diluted 1 50 with PBX-5% normal horse serum. They are rinsed in 0.1 M sodium phosphate buffer and then incubated for 1 hr in peroxidase antiperoxidase (PAP), diluted 1 100 with PBX. The sections are rinsed three times for 5 min each in the same buffer followed by distilled water rinses. They are incubated for 10 min in 50 ml of 0.05 M imidazole/0.05 M cacodylate buffer (pH 7.2) containing 50 mg of DAB. This is followed by an additional 10 min incubation after adding 200 xl H202. All incubations are carried out under constant agitation. The sections are washed in distilled water, placed in the same buffer, mounted onto gelatin-coated slides, dried, dehydrated, and cover-slipped with Permount. Note that the ABC procedure can be used instead of the PAP procedure. 

Give the formulas of primary, secondary, and tertiary sodium phosphates. State how the solution of each behaves with litmus. 

Fig. 14.3. Secondary structural changes of prion protein, (32-microglobulin and a-synuclein upon UV exposure under their respective amyloid-forming conditions. Far UV CD spectra of (a) prion protein in 20 mM sodium phosphate buffer (pH 6.8) containing 100 mM NaCl, 3M urea and 1M GdmCl. Inset shows the Far UV CD spectrum of native prion protein (b) (32-microglobuhn in 50 mM citrate buffer (pH 2.5) containing 100mM KC1 and (c) a-synuclein in 20 mM 11EPES- NaOl I buffer (pH 7.0) containing 100 mM NaCl and 0.5 mM SDS. In each panel, curves 1 and 2 show the far UV CD spectra of the protein before and after exposure to UV light, respectively. Panel 3a reproduced from [3]...

Biotinylated secondary antibody 3 pg/mL, in diluent. Avidin-conjugated peroxidase 1.0 pg/mL, in diluent. Citrate-phosphate buffer (pH 5) Mix equal vol of O.IM citric acid and 0.2Mdibasic sodium phosphate, ind dilute 1 1 with distilled water. Substrate solution Add 2.5 mg of 2,2 azino-Ws(3-ethylbenz-thiazoline-6-sulfonic acid) to 10 mL of citrate-phosphate buffer. Add 10 pL of 30% hydrogen peroxide to this solution. Make fresh as required. 

A. Schwarzenberg made monocHnic prisms of disodium diammonium pyro-phosphate Na2(NH4)2P207, by evaporating a mixture of secondary sodium pyrophosphate and aqua ammonia over quicklime and ammonium chloride. The crystals are readily soluble in water, and the soln., when boiled, loses ammonia. A. Schwarzenberg prepared crystals of hemihydratM dipotassium ammonium hydropyrophosphate, K2(NH4)HP207.JH20. 

Mobile phases The primary mobile phase for the pretreatment column was a mixture of 1/15 M sodium phosphate solution (adjusted to pH 3.5 with 1/15 M phosphoric acid) and methanol (48 52). The secondary mobile phase for the analytical column was the primary mobile phase containing 17.5 mM SDS. The tertiary mobile phase was the primary mobile phase containing 175 mM SDS. The flow rates of the primary, secondary and tertiary mobile phases were 0.9, 1.0 and 0.1 ml min-1 respectively. 

The isolation of D1 protein was conducted as mild as possible in order to isolate the D1 protein without loss of secondary acceptor of electrons- plastoquinone Qp. The D1 protein and BSA were dissolved in 100 mM sodium phosphate saline buffer (PBS) at the concentrations 5 mg/ml to prepare relatively thick (10-50 pm) gel-like films containing the protein. A drop of resulting mixture was cast onto Si-Si02-Si3N4 (silica nitride) surface and then they were exposed to glutaraldehyde vapors in a closed vessel for 30 minutes at + 10 C. After that, samples were rinsed in PBS for 30 min. 

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