Oxygen reduction on iron—V. Processes in boric acid-borate buffer solutions in the 7.4–9.8 pH range

1991 ◽  
Vol 32 (5-6) ◽  
pp. 563-576 ◽  
Author(s):  
S Zečević ◽  
D.M Draẑić ◽  
S Gojkovć
Keyword(s):  
Boric Acid ◽  
Oxygen Reduction ◽  
Borate Buffer ◽  
Buffer Solutions ◽  
Ph Range

scholarly journals THE KINETICS OF SAPONIFICATION OF IODOACETIC ACID BY SODIUM HYDROXIDE AND BY CERTAIN ALKALINE BUFFER SOLUTIONS

1936 ◽  
Vol 19 (6) ◽  
pp. 899-906 ◽  
Author(s):  
R. Brdička
Keyword(s):  
Ionic Strength ◽  
Boric Acid ◽  
Sodium Hydroxide ◽  
Salt Effect ◽  
Iodoacetic Acid ◽  
Borate Buffer ◽  
Polarographic Method ◽  
Buffer Solutions ◽  
Glycollic Acid ◽  
Kinetics Of

1. The rate of the saponification of iodoacetic acid in sodium hydroxide and alkaline buffer solutions yielding glycollic acid was measured by means of Heyrovský's polarographic method. 2. From the bimolecular velocity constants, increasing with the ionic strength of the solution, the Brönsted factor, F, which characterizes the primary salt effect, was calculated. 3. In the borate buffer solutions the monomolecular constants of the saponification were determined which, at values above the pH of neutralization of boric acid, show a proportionality to the concentration of hydroxyl anions. Below the pH of neutralization of boric acid, they are proportional to the concentration of borate anions.

scholarly journals Electrochemical Behaviour of N′-(p-toluenesulphonyl)-3-methyl-4-(4′-substituted arylhydrazono) pyrazolin-5-ones

2012 ◽  
Vol 9 (4) ◽  
pp. 1864-1874
Author(s):  
V. Nagaraju ◽  
R. Sreenivasulu ◽  
P. Venkata Ramana
Keyword(s):  
Electrochemical Behaviour ◽  
Reduction Process ◽  
Effect Of Solvent ◽  
Buffer Solutions ◽  
Diffusion Controlled ◽  
Controlled Potential Electrolysis ◽  
Dc Polarography ◽  
Controlled Potential ◽  
Ph Range ◽  
And Diffusion

The electrochemical behaviour of N′-(p-toluenesulphonyl)-3-methyl-4-(4′-substituted arylhydrazono) pyrazolin-5-ones has been investigated at dme and gc electrodes in buffer solutions of pH 2.0, 4.0, 6.0, 8.0 and 10.0 using dc polarography and cyclic voltammetry and coulometry. The compounds exhibit one well defined wave in the entire pH range of study. The process is irreversible and diffusion controlled. Controlled potential electrolysis indicates the involvement of four electrons in the reduction process. The effect of solvent, cations and anions, temperature and substitutents on the mechanism of reduction has been studied. Based on the results obtained the mechanism of reduction has been suggested.

scholarly journals Purification and properties of β-N-acetylhexosaminidase from the mollusc Helicella ericetorum Müller

1978 ◽  
Vol 175 (2) ◽  
pp. 743-750 ◽  
Author(s):  
P Calvo ◽  
A Reglero ◽  
J A Cabezas
Keyword(s):  
Active Site ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Mixed Substrates ◽  
Ph Optimum ◽  
Terrestrial Mollusc ◽  
Buffer Solutions ◽  
Purification And Properties ◽  
Competitive Inhibitors ◽  
Ph Range

1. A beta-N-acetylhexosaminidase was purified 330-fold from the digestive gland of the terrestrial mollusc Helicella ericetorum Müller. 2. Its pH optimum is 4.5 for both beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities in two buffer solutions; it is fully stable at 37 degrees C for 2h in the pH range 3.8–4.6 and shows one isoelectric point (pH 4.83). 3. The estimated mol.wt. is between 120,000 and 145,000. 4. The enzyme shows an endo-beta-N-acetylhexosaminidase activity on natural substrates such as ovalbumin, ovomucoid, chondroitin 4-sulphate, chitin and hyaluronic acid. 5. Two forms of the enzyme were separated by preparative polyacrylamide-gel electrophoresis. 6. Km and Vmax. for p-nitrophenyl 2-acetamido-2-deoxy-beta-D-glucopyranoside and p-nitrophenyl 2-acetamide-2-deoxy-beta-D-galactopyranoside are 0.43 mM, 30.1 micronmol of p-nitrophenol/min per mg and 0.19 mM, 8.6 micronmol of p-nitrophenol/min per mg respectively. 7. It is inhibited by Hg2+, Fe3+, acetate, some lactones, N-acetylgalactosamine, N-acetylglucosamine and mannose. 8. Mixed-substrates analysis and Ki values for competitive inhibitors indicated that beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities are catalysed by the enzyme at the same active site.

STUDIES ON THE ADSORPTION OF BORON ON HUMIC ACIDS

1990 ◽  
Vol 70 (3) ◽  
pp. 305-311 ◽  
Author(s):  
BAOHUA GU ◽  
L. E. LOWE
Keyword(s):  
Boric Acid ◽  
Humic Acids ◽  
Organic Matter Content ◽  
Langmuir Adsorption Isotherm ◽  
Matter Content ◽  
Langmuir Equation ◽  
Langmuir Adsorption ◽  
Ph Values ◽  
Ph Range

The adsorption of B, in the form of boric acid, was studied on three precipitated humic acids (HA), representing three distinct soil types. B adsorption by HA was strongly pH-dependent, being low and relatively constant in the pH range 3.0–6.5, increasing markedly up to a peak at near pH 9.5, and then decreasing at still higher pH values. Adsorption isotherms for pH values near 6.7 and 8.8 conformed well to the Langmuir equation. The adsorption maxima (b values), as calculated with the Langmuir equation, ranged from 73 to 207 mmol kg−1 HA at a pH near 8.8, and from 10 to 42 mmol kg−1 at a pH near 6.7. The considerable variation in B adsorption by these HA samples was attributed to "Fe + Al" contents present as contaminants in the HA. The role of HA in B adsorption is expected to be minor in most acid and near neutral soils, but may be of greater significance in soils of high pH and above average organic matter content. Key words: Boron adsorption, boric acid, humic acid, Langmuir adsorption isotherm.

(Invited) Micro- and Nano-Structure of Passive Film Formed on High Strengthen Steel Surface in pH 6.5 Boric Acid-Borate Buffer Solution

2020 ◽  
Vol MA2020-02 (12) ◽  
pp. 1263-1263
Author(s):  
Koji Fushimi ◽  
Kanta Higa ◽  
Yuichi Kitagawa ◽  
Yasuchika Hasegawa ◽  
Hideki Katayama
Keyword(s):  
Boric Acid ◽  
Passive Film ◽  
Steel Surface ◽  
Borate Buffer ◽  
Borate Buffer Solution ◽  
Buffer Solution ◽  
Nano Structure
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