Effect of phosphate salts concentrations, supporting electrolytes, and calcium phosphate salt precipitation on the pH of phosphate buffer solutions

2009 ◽  
Vol 278 (1-2) ◽  
pp. 76-84 ◽  
Author(s):  
Yoonjee Park ◽  
Sook Heun Kim ◽  
Sadis Matalon ◽  
Nien-Hwa Linda Wang ◽  
Elias I. Franses
Keyword(s):  
Calcium Phosphate ◽  
Phosphate Buffer ◽  
Salt Precipitation ◽  
Buffer Solutions ◽  
Phosphate Salts

scholarly journals Enhanced bleaching effect of bovine tooth by hydrogen peroxide via calcium phosphate spheres

2018 ◽  
Keyword(s):  
Hydrogen Peroxide ◽  
Calcium Phosphate ◽  
Hydrothermal Method ◽  
Phosphate Buffer ◽  
Bleaching Effect ◽  
Whitening Effect ◽  
Buffer Solutions

In the study, calcium phosphate spheres (CPS) were prepared using phosphate buffer solutions by hydrothermal method and were used to manufacture a lab-made bleaching paste. The obtained paste was used to whiten bovine teeth in order to investigate whitening effect with CPS in the paste. The results showed that the bleaching paste made by CPS does not affect bleaching effect of hydrogen peroxide (HP). On the contrary, it can prolong the bleaching effect compared the pure HP.

scholarly journals OBSERVATIONS IMPLICATING AN EXTRACELLULAR ENZYMIC MECHANISM OF CONTROL OF BONE MORPHOGENESIS

1974 ◽  
Vol 22 (2) ◽  
pp. 88-103 ◽  
Author(s):  
MARSHALL R. URIST ◽  
HISASHI IWATA ◽  
STUART D. BOYD ◽  
PETER L. CECCOTTI ◽  
MARLYS OKADA ◽  
...  
Keyword(s):  
Chemical Reactions ◽  
Phosphate Buffer ◽  
Bone Matrix ◽  
Chemical Extraction ◽  
Ammonium Bromide ◽  
Property A ◽  
Noncollagenous Proteins ◽  
Buffer Solutions ◽  
Sequential Chemical Extraction ◽  
Chloroform Methanol

Data on physicochemical conditions leading to loss of the bone morphogenetic property of bone matrix in neutral buffer solutions support the concept of an enzymic control mechanism better than a chemical blocking reaction or denaturation. The loss is associated with release of 35S-labeled constituents and not prevented by ε-amino caproic acid, an inhibitor of cathepsins. The loss is also associated with release of 35S-cysteine-labeled protein; about 60% of the yield is sustained by the addition of only 3 mmoles/liter of iodoacetic acid. A latent period of about 12 hr, decreased by extraction of bone matrix with CaCl2, is characterized by release of protein polysaccharide and other noncollagenous proteins. Release of sialic acid from the bone matrix by neuraminidase at pH 7.4 has no effect upon bone yield. At 2°C, Tris-HCl buffer or ethylenediaminetetraacetic acid extracts noncollagenous proteins without loss of bone yield; at 37°C, pH 7.4, these solutions also activate endogenous enzymes and reduce bone yield. The component of bone matrix responsible for reduction in bone yield is separable from bone matrix by extraction with phosphate buffer, by catheptic digestion of bone matrix in acidic buffer solutions, by sequential chemical extraction of noncollagenous proteins with cold slightly acidic salt solutions or by extraction-denaturation with chloroform-methanol. Detergents neither extinguish nor denature the morphogenetic property but some solubilize or extract degradative enzymes; hexodecyl trimethyl ammonium bromide, at pH 5.0, is positively charged and extracts hydrophobic proteins, including part of the bone morphogenetic property. A special selection of sulfhydryl chemical inhibitors remarkably different from the selection inhibiting known enzymes preserves the bone morphogenetic property of bone matrix; p-chloromercuribenzoate preservation is reversible by chemical reactions with cysteine. Reduction in bone yield in phosphate buffer is not attributable to a chemical block because chloroform-methanol extraction of the agent does not restore bone yield and is not attributable to denaturation because bone yield sustained by p-chloromercuribenzoate is lost by chemical reactions with cysteine. An hypothetical insoluble bone morphogenetic protein (BMP) firmly bound to collagen is degraded by a soluble neutral proteinase (BMPase). Digestion of the hypothetical BMP occurs without loss of the 640-A electron micrographic image of bone collagen, resembles tryptic digestion and is more selective as well as physiologic in action.

Molecular Basis of Salivary Proline-rich Protein and Peptide Synthesis: Cell-free Translations and Processing of Human and Macaque Statherin mRNAs and Partial Amino Acid Sequence of their Signal Peptides

1987 ◽  
Vol 66 (2) ◽  
pp. 462-466 ◽  
Author(s):  
F.G. Oppenheim ◽  
D.I. Hay ◽  
D.J. Smith ◽  
G.D. Offner ◽  
R.F. Troxler
Keyword(s):  
Calcium Phosphate ◽  
Macaca Fascicularis ◽  
Electrophoretic Analysis ◽  
Proteolytic Processing ◽  
Oral Environment ◽  
Reticulocyte Lysate ◽  
Polyprotein Precursor ◽  
Phosphate Salts ◽  
Calcium Phosphate Precipitation

Acidic proline-rich phosphoproteins and phosphopeptides are abundant components of parotid and submandibular salivary secretions in man and in the subhuman primate, Macaca fascicularis. The major acidic proline-rich proteins and the proline-rich phosphopeptide, statherin, of man and macaques have been shown to be potent inhibitors of calcium phosphate precipitation and are thought to function in the oral environment by maintaining saliva supersaturated with respect to calcium phosphate salts. Little is known about the biosynthesis of these proline-rich phosphoproteins and peptides, and the aim of the present work was to determine the structural relationship between statherin precursors and native human and macaque statherin. RNA was isolated from human submandibular gland, and poly(A+) mRNA was selected by affinity chromatography on oligo(dT) cellulose and translated in a reticulocyte lysate. Electrophoretic analysis of the translation products revealed that this mRNA directed the synthesis of a large number of polypeptides with M,s ranging from 5000 to 70,000. Immunoprecipitates, prepared with an antiserum directed against human statherin, contained a single component with a Mr of 7800, approximately 2000 daltons larger than native statherin. Radiosequencing of the in vitro precursor of statherin in immunoprecipitates demonstrated the presence of a 19-residue signal peptide. These results suggest that statherin is derived from a unique structural gene, and does not result from proteolytic processing of a large polyprotein precursor.

Wet chemical porosification with phosphate buffer solutions for permittivity reduction of LTCC substrates

2020 ◽  
pp. 158059
Author(s):  
Ali Hajian ◽  
Thomas Konegger ◽  
Konrad Bielecki ◽  
Bjoern Mieller ◽  
Torsten Rabe ◽  
...  
Keyword(s):  
Phosphate Buffer ◽  
Buffer Solutions ◽  
Wet Chemical

scholarly journals THE PROPERTIES OF MAMMALIAN STRIATED MYOFIBRILS ISOLATED BY AN ENZYMATIC METHOD

1950 ◽  
Vol 91 (6) ◽  
pp. 655-664 ◽  
Author(s):  
Armin F. Schick ◽  
George M. Hass
Keyword(s):  
Ionic Strength ◽  
Potassium Chloride ◽  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Microscopic Structure ◽  
Buffer Solution ◽  
Buffer Solutions ◽  
Alkaline Side ◽  
Fresh Frozen

A new method for the isolation of large numbers of individual myofibrils from fresh mammalian skeletal and cardiac muscle has been described. Purification of isolated myofibrils was accomplished by differential centrifugation of fresh frozen sections of muscle which had been mechanically agitated after exposure for 30 to 45 minutes at 0°C. to the action of a dilute solution of trypsin in a phosphate buffer solution with a pH of 7.0 and an ionic strength of 0.25. Isolated skeletal myofibrils of the rabbit and man have similar constant solubility properties. They dissolve in an aqueous mixture of 0.5 N potassium chloride and 0.03 N sodium bicarbonate, giving viscous solutions which exhibit conspicuous birefringence of flow. They are soluble in buffer solutions (ionic strength 0.15) on the acid side of pH 4 and alkaline side of pH 10. If the ionic strength of potassium phosphate buffer solutions is increased to 0.5 or if the ionic strength of phosphate-borate buffer solutions is increased to a similar value by addition of potassium chloride, the isolated myofibrils become soluble at neutrality. Hence, it is possible, first to isolate the myofibrils and then dissolve them without deviating appreciably from physiologic ranges of pH. The extent to which myofibrils are modified by the conditions imposed by the method of isolation is unknown. There is no significant change in microscopic structure or optical birefringence. Furthermore, there is retention of a form of physiological reactivity, for when the isolated skeletal myofibrils are immersed in solutions of adenosinetriphosphate, they promptly and irreversibly change from elongated fibrils with distinct structural detail into dense spherical masses without recognizable microscopic structure.

Chemical specificity of a laryngeal apneic reflex in puppies

1982 ◽  
Vol 53 (2) ◽  
pp. 455-462 ◽  
Author(s):  
D. F. Boggs ◽  
D. Bartlett
Keyword(s):  
Phosphate Buffer ◽  
Superior Laryngeal Nerve ◽  
Critical Factor ◽  
Laryngeal Nerve ◽  
Sodium Salts ◽  
Single Fibers ◽  
Buffer Solutions ◽  
Chloride Salts ◽  
Cation Substitutions ◽  
Stimulation Of

In neonatal mammals the introduction of water and some other fluids into the larynx causes prolonged reflex apnea by stimulation of afferents in the superior laryngeal nerve (SLN). We have studied the chemical specificity of this reflex in 1- to 9-day-old anesthetized puppies. The laryngeal lumen was perfused with a variety of substances while ventilation through a tracheal cannula was recorded. Water consistently elicited apnea, which was terminated by 150 mM NaCl. Sucrose and urea solutions (100–500 mM) also elicited apnea, suggesting that osmolarity is not a critical factor. Phosphate buffer solutions containing NaCl and ranging in pH from 4.5 to 8.7 did not elicit apnea nor did cation substitutions in 150 mM chloride salts, with the exception of K+. Anion substitutions in 150 mM sodium salts indicated that anions of relatively large hydrated size (F-, acetate, formate, gluconate, tartrate, SO2–4, diatrizoate, IO-3, BrO-3, H2PO-4, HCO-3, borate, CO2–3) do induce apnea, whereas small anions (NO-3, ClO-3, SCN-, I-, Br-) similar to Cl- in size do not. Large anion salts and the nonelectrolytes sucrose, urea, and milk ceased to be effective stimuli in the presence of Cl- in concentrations of 80 or more meq/l. The principal stimulus for this apneic reflex is thus the absence or reduced concentration of Cl- (or small anions that can functionally replace Cl-) in the laryngeal fluid. Single fibers in the SLN were responsive to all the substances found capable of eliciting apnea and unresponsive to those not capable of doing so.

scholarly journals pH-sensitive polyvinylpyrrolidone-acrylic acid hydrogels: Impact of material parameters on swelling and drug release

2014 ◽  
Vol 50 (1) ◽  
pp. 173-184 ◽  
Author(s):  
Kashif Sohail ◽  
Ikram Ullah Khan ◽  
Yasser Shahzad ◽  
Talib Hussain ◽  
Nazar Muhammad Ranjha
Keyword(s):  
Drug Release ◽  
Acrylic Acid ◽  
Phosphate Buffer ◽  
Ph Sensitive ◽  
Cross Linking ◽  
Release Mechanism ◽  
Effect Analysis ◽  
X Ray Crystallography ◽  
Buffer Solutions ◽  
The One

In this study, we fabricated pH-sensitive polyvinylpyrrolidone/acrylic acid (PVP/AA) hydrogels by a free-radical polymerisation method with variation in the content of monomer, polymer and cross-linking agent. Swelling was performed in USP phosphate buffer solutions of pH 1.2, 5.5, 6.5 and 7.5 with constant ionic strength. Network structure was evaluated by different parameters and FTIR confirmed the formation of cross-linked hydrogels. X-ray crystallography showed molecular dispersion of tramadol HCl. A drug release study was carried out in phosphate buffer solutions of pH 1.2, 5.5 and 7.5 for selected samples. It was observed that swelling and drug release from hydrogels can be modified by changing composition and degree of cross-linking of the hydrogels under investigation. Swelling coefficient was high at higher pH values except for the one containing high PVP content. Drug release increased by increasing the pH of the medium and AA contents in hydrogels while increasing the concentration of cross-linking agent had the opposite effect. Analysis of the drug release mechanism revealed non-Fickian transport of tramadol from the hydrogels.

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