KINETIC STUDIES ON METHYL-BIS-β-CHLOROETHYLAMINE: V. THE REACTIONS IN VARIOUS ACID SOLUTIONS

1948 ◽  
Vol 26b (2) ◽  
pp. 193-201
Author(s):  
C. A. Winkler ◽  
T. J. Hardwick ◽  
A. L. Thompson
Keyword(s):  
Kinetic Studies ◽  
Chloride Ions ◽  
Ammonium Salts ◽  
Acid Solutions ◽  
Hydrogen Ions ◽  
Kinetics Of Hydrolysis ◽  
Hydroxyl Ion ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Direct Attack

The hydrolysis of the quaternary ammonium salts of methyl-bis-β-chloroethylamine is inhibited by both hydrogen ions and chloride ions. I he kinetics of hydrolysis in various anion solutions suggest that reaction occurs by direct attack at the β-chlorine atoms by hydroxyl ion.

scholarly journals Kinetic studies on glucoamylase of rabbit small intestine

1976 ◽  
Vol 153 (2) ◽  
pp. 321-327 ◽  
Author(s):  
S Sivakami ◽  
A N Radhakrishnan
Keyword(s):  
Small Intestine ◽  
Substrate Specificity ◽  
Kinetic Studies ◽  
Kinetic Properties ◽  
Ph Optimum ◽  
Kinetics Of Hydrolysis ◽  
Brush Borders ◽  
Rabbit Small Intestine ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetic properties of a maltase-glucoamylase complex with a neutral pH optimum, purified to homogeneity from the brush borders of the rabbit small intestine, are described. It has a broad range of substrate specificity, hydrolysing di- and poly-saccharides with α-1,4 and α-1,6 linkages. The Km and Vmax, values of the enzyme for the various substrates were determined. Starch and maltose were its best substrates. The kinetics of hydrolysis of two synthetic linear maltosaccharides, namely maltotriose and maltopentaose, were studied. Mixed-substrate incubation studies revealed the presence of at least two interacting sites on the enzyme, and the data were further analysed by the use of a number of non-substrate inhibitors.

Kinetics of hydrolysis of o-aminomethylphenols and their ammonium salts

1982 ◽  
Vol 31 (1) ◽  
pp. 72-75
Author(s):  
A. B. Teitel'baum ◽  
L. A. Kudryavtseva ◽  
V. E. Bel'skii ◽  
V. E. Ivanov
Keyword(s):  
Ammonium Salts ◽  
Kinetics Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

Kinetics of hydrolysis of peroxodisulphate ions in acidic medium to peroxomonosulphuric acid

1981 ◽  
Vol 46 (5) ◽  
pp. 1229-1236 ◽  
Author(s):  
Jan Balej ◽  
Milada Thumová
Keyword(s):  
Ionic Strength ◽  
Rate Constants ◽  
Acidic Medium ◽  
Measured Data ◽  
Molar Ratios ◽  
Starting Solution ◽  
Kinetics Of Hydrolysis ◽  
Rate Of Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

The rate of hydrolysis of S2O82- ions in acidic medium to peroxomonosulphuric acid was measured at 20 and 30 °C. The composition of the starting solution corresponded to the anolyte flowing out from an electrolyser for production of this acid or its ammonium salt at various degrees of conversion and starting molar ratios of sulphuric acid to ammonium sulphate. The measured data served to calculate the rate constants at both temperatures on the basis of the earlier proposed mechanism of the hydrolysis, and their dependence on the ionic strength was studied.

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