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Stability constants for some 1 : 1 metal-carboxylate complexes
Stability constants have been measured for the formation of 1:1 complexes between eight divalent metal ions and six carboxylate anions. For each anion the stabilities of the complexes follow the
The dependence of initial velocity upon substrate concentration has been examined in the carboxypeptidase A catalyzed hydrolysis of the following hippuric acid esters (at pH 7.5, 25°, ionic strength
Substrate Activation in the Carboxypeptidase A Catalysis of Ester Hydrolysis
The hydrolyses of the O-hippuryl derivatives of glycolic acid (1a), 2-methyllactic acid (1b), and p-chloromandelic acid (1c) by bovine carboxypeptidase A display substrate activation. The hydrolyse...
The Hydrolysis of Benzoate Esters by Carboxypeptidase A and the pH-Rate Profile for the Hydrolysis of O-Hippuryl-L-3-phenyllactic Acid
A series of para-substituted O-benzoyl-2-hydroxybutanoic acids (but not the unsubstituted ester) are hydrolyzed by bovine carboxypeptidase A (pH 7.5, ionic strength 0.5, 25°). For the CH3O, CH3, Cl,
Nucleophilicity towards a saturated carbon atom: rate constants for the aminolysis of methyl 4-nitrobenzenesulfonate in aqueous solution. A comparison of the n and N+ parameters for amine
Second-order rate constants (kNu) have been measured in aqueous solution (I= 0.1 mol dm –3, 25 °C) for the SN2 reactions of methyl 4-nitrobenzenesulfonate with ammonia, 41 primary amines, 20
pH dependence of the hydrolysis of hippuric acid esters by carboxypeptidase A.
The pH dependence (pH 4.5-10.5) of the hydrolysis of seven hippuric acid esters by bovine carboxypeptidase A has been investigated, and the pH dependence of the substrate activation of 1a-c and the substrate inhibition of 1d-g have been compared.
Reversible Inhibition of the Esterase Activity of Carboxypeptidase A by Carboxylate Anions
Reversible inhibition of the hydrolysis of O-(hippuryl)-L-3-phenyllactic acid by carboxypeptidase A has been studied for 26 carboxylate ion inhibitors at 25°, pH 7.5, and ionic strength 0.2 (NaCl).
Evolution of self-organization in nano-structured PVD coatings under extreme tribological conditions
Abstract The evolution of the self-organization process where dissipative structures are formed under the extreme frictional conditions associated with high performance dry machining of hardened
Reversible Inhibition of Carboxypeptidase A. IV. Inhibition of Specific Esterase Activity by Hippuric Acid and Related Species and other Amino Acid Derivatives and a Comparison with Substrate
The anions of each of the following carboxylic acids exhibit uncompetitive inhibition of the hydrolysis of O-hippuryl-L-3-phenyllactic acid by bovine carboxypeptidase A at pH 7.5, 25°, ionic streng...