scholarly journals Stability of Indomethacin in Aqueous Solution. (1): Kinetic Studies and Effect of Solvents on the Hydrolysis of Indomethacin.

1992 ◽  
Vol 18 (1) ◽  
pp. 43-51 ◽  
Author(s):  
KAORU CHIBA ◽  
MASANAO TAKAHASHI ◽  
NOBUMASA HAYASE ◽  
SHIGETAKA AKUTSU ◽  
SHUNICHI INAGAKI
1982 ◽  
Vol 35 (7) ◽  
pp. 1357 ◽  
Author(s):  
TJ Broxton

The hydrolysis of 2-acetyloxybenzoic acid in the pH range 6-12 has been studied in the presence of micelles of cetyltrimethylammonium bromide (ctab) and cetylpyridinium chloride (cpc). In the plateau region (pH 6-8) the hydrolysis is inhibited by the presence of micelles, while in the region where the normal BAC2 hydrolysis (pH > 9) occurs the reaction is catalysed by micelles of ctab and cpc. The mechanism of hydrolysis in the plateau region is shown to involve general base catalysis by the adjacent ionized carboxy group both in the presence and absence of micelles. This reaction is inhibited in the presence of micelles because the substrate molecules are solubilized into the micelle and water is less available in this environment than in normal aqueous solution.


1977 ◽  
Vol 32 (1-2) ◽  
pp. 101-109 ◽  
Author(s):  
Franz J. Fehrenbach ◽  
Hansjörg Eibl

1. Kinetic studies on the binding of 125I-Streptolysin-O exhibited immediate fixation of activated toxin to natural and artificial membranes. Once fixed to the membrane no release of Streptolysin-O or Streptolysin-O-lipid-complexes has been observed. 2. In contrast to activated toxin (free SH-groups!), oxidized Streptolysin-O was shown to become also fixed to membranes, however, with different binding kinetics. The binding of oxidized material was clearly dependent on temperature and time. When the toxin was oxidized twice the amount of labelled material was bound as compared with the hemolytically active Streptolysin-O. This suggests that oxidized Streptolysin-O, too, possesses a “binding site” within the molecule, though free SH-groups were expected to be essential for toxin fixation at the membrane. It has been shown that oxidized (inactive) and reduced (active) Streptolysin-O forms stable “complexes” with liposomes in aqueous solution, which could be separated by chromatography on Sepharose gels. 3. The binding of 125I-toxin to membranes and liposomes was specific since specific antisera against Streptolysin-O inhibited fixation of toxin completely. 4. Hydrolysis of phospholipids and release of lysophosphatides by Streptolysin-O esterase (EC 2.1.1.2) has not been observed, thus providing no evidence for an enzymatic concept of membrane damage.


Author(s):  
Xiaoyan Wang ◽  
Jinmei Du ◽  
Changhai Xu

Abstract:: Activated peroxide systems are formed by adding so-called bleach activators to aqueous solution of hydrogen peroxide, developed in the seventies of the last century for use in domestic laundry for their high energy efficiency and introduced at the beginning of the 21st century to the textile industry as an approach toward overcoming the extensive energy consumption in bleaching. In activated peroxide systems, bleach activators undergo perhydrolysis to generate more kinetically active peracids that enable bleaching under milder conditions while hydrolysis of bleach activators and decomposition of peracids may occur as side reactions to weaken the bleaching efficiency. This mini-review aims to summarize these competitive reactions in activated peroxide systems and their influence on bleaching performance.


1983 ◽  
Vol 29 (8) ◽  
pp. 1513-1517 ◽  
Author(s):  
M W McGowan ◽  
J D Artiss ◽  
B Zak

Abstract A procedure for the enzymatic determination of lecithin and sphingomyelin in aqueous solution is described. The phospholipids are first dissolved in chloroform:methanol (2:1 by vol), the solvent is evaporated, and the residue is redissolved in an aqueous zwitterionic detergent solution. The enzymatic reaction sequences of both assays involve hydrolysis of the phospholipids to produce choline, which is then oxidized to betaine, thus generating hydrogen peroxide. The hydrogen peroxide is subsequently utilized in the enzymatic coupling of 4-aminoantipyrine and sodium 2-hydroxy-3,5-dichlorobenzenesulfonate, an intensely red color being formed. The presence of a non-reacting phospholipid enhances the hydrolysis of the reacting phospholipid. Thus we added lecithin to the sphingomyelin standards and sphingomyelin to the lecithin standards. This precise procedure may be applicable to determination of lecithin and sphingomyelin in amniotic fluid.


1971 ◽  
Vol 26 (6) ◽  
pp. 543-545
Author(s):  
Leopoldo J. Anghileri ◽  
Esther S. Miller

The hydrolysis of 32P-sodium polyphosphates (linear and cross-linked) in aqueous solution has been studied. The radiometric determinations indicate that the ortho-phosphate formation is a slow reaction, and that the amount formed by the linear variety is higher than that produced by the cross-linked form. There is a significant formation of metaphosphates during the hydrolysis of the cross-linked polyphosphate which is missing or at least reduced to a much lesser extent in the case of the linear polyphosphate.


1965 ◽  
Vol 18 (5) ◽  
pp. 651 ◽  
Author(s):  
RW Green ◽  
PW Alexander

The Schiff base, N-n-butylsalicylideneimine, extracts more than 99.8% beryllium into toluene from dilute aqueous solution. The distribution of beryllium has been studied in the pH range 5-13 and is discussed in terms of the several complex equilibria in aqueous solution. The stability constants of the complexes formed between beryllium and the Schiff base are log β1 11.1 and log β2 20.4, and the distribution coefficient of the bis complex is 550. Over most of the pH range, hydrolysis of the Be2+ ion competes with complex formation and provides a means of measuring the hydrolysis constants. They are for the reactions: Be(H2O)42+ ↔ 2H+ + Be(H2O)2(OH)2, log*β2 - 13.65; Be(H2O)42+ ↔ 3H+ + Be(H2O)(OH)3-, log*β3 -24.11.


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